Acrylamide-degrading microorganisms.
\r\n\tWeather warnings released all over the world as well as the regional level even on the country level, which is important forecasts. They use it to protect life and property. The weather forecasting is playing an important role in planning and management to save the infrastructure and people's lives from disasters. Weather forecasting determines the atmosphere process in the future. It is related to understanding the atmospheric process through observed and remote sensing meteorology data. We can say the collecting as much as data as possible about the current state of the atmosphere particularly the temperature, humidity, and wind. There is a vast variety of end uses to weather forecasts. There is a number of methods i.e. statistically, numerical, artificial neural network, and different weather forecasting models. Climate change increases the demand for weather forecasting. Due to weather forecasts, decision-makers can take different protective measures in every field of life especially agriculture regarding food hunger. The extreme event of weather impact on agriculture as well as infrastructure.
",isbn:"978-1-83968-054-0",printIsbn:"978-1-83968-053-3",pdfIsbn:"978-1-83968-055-7",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,hash:"eadbd6f9c26be844062ce5cd3b3eb573",bookSignature:"Associate Prof. Muhammad Saifullah",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/8485.jpg",keywords:"Global, Regional, Weekly, Daily, Meteorology, Satellite Product, Statistics Models, Artificial Neural Network Model, Climate Change, Economic Values, Future Farming, Food Security",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:0,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"October 14th 2020",dateEndSecondStepPublish:"November 23rd 2020",dateEndThirdStepPublish:"January 22nd 2021",dateEndFourthStepPublish:"April 12th 2021",dateEndFifthStepPublish:"June 11th 2021",remainingDaysToSecondStep:"2 months",secondStepPassed:!0,currentStepOfPublishingProcess:3,editedByType:null,kuFlag:!1,biosketch:"A researcher in the field of hydrology and water resources. He also separated the impact of climate change and human activities on runoff in Indus and Yellow River. He has a very good command of numerical modeling of surface water, groundwater, and glaciers hydrology.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"320968",title:"Associate Prof.",name:"Muhammad",middleName:null,surname:"Saifullah",slug:"muhammad-saifullah",fullName:"Muhammad Saifullah",profilePictureURL:"https://mts.intechopen.com/storage/users/320968/images/system/320968.jpg",biography:"Dr.Saifullah has vast experience in the field of hydrology, water resources, climate change, and weather. He also won the award best research scholar at Hohai University of 2016 from the Ministry of education as well as second position in the Yellow river Hydraulic Research Institute. 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It is soluble in water, methanol, ethanol, dimethyl ether, and acetone, but insoluble in benzene and heptane. Acrylamide is incompatible with acids, bases, oxidizing agents, irons and iron salts. It decomposes non-thermally to form ammonia while thermal decomposition produces carbon monoxide, carbon dioxide, and oxides of nitrogen [1].
As a commercial conjugated reactive molecule, acrylamide has been used worldwide for the synthesis of polyacrylamide and other polymers [2, 3]. It has also been used as a binding, thickening, or flocculating agent in grout, cement, sewage, wastewater treatment, pesticide formulation, cosmetics, sugar manufacturing, and to prevent soil erosion. Polymers of this compound have been used in ore processing, food packaging, plastic products, and in scientific and medical laboratories as solid support for the separation of proteins by electrophoresis [4]. Acrylamide monomer is also widely used as an alkylating agent for the selective modification of sulfhydryl proteins and in fluorescence studies of tryptophan residues in proteins. In 2002, there was an alarming report of the occurrence of acrylamide at high levels up to 3 mg/kg in plant-derived foods and thought to form during cooking allowing the formation of Maillard browning products [5]. Many reports have suggested that acrylamide seems to be found in foods that have been processed by heat-treatment methods other than boiling [6]. One possible pathway to the formation of acrylamide is via the Maillard reaction between amino acids, particularly asparagines, and reducing sugars at high temperatures [5, 6]. Some reports suggest acrylamide could form by acrolein (2-propenal, CH=CHCHO), a three-carbon aldehyde, by either the transformation of lipids or the degradation of amino acids, proteins and carbohydrates [7-12].
Acrylamide could be absorbed through unbroken skin, mucous membranes, lungs, and the gastrointestinal tract. Human exposure to acrylamide is primarily occupational from dermal contact with the solid monomer and inhalation of dust and vapor. Although it is not toxic in polymer form, the monomer can cause peripheral neuropathy. Residual monomer in polymers is also of health concern [13]. Primary exposure occurs during the handling of monomers. Two acrylamide manufacturing factories showed breathing zone concentrations of 0.1 to 3.6 mg/m3 [1]. During normal operations, workers at another plant were exposed to not more than 0.3 mg/m3. Aside from occupational exposure, probable exposure to the general public is through consumption of certain foods [14]. Another source of acrylamide exposure to the general public could be through drinking water treated with polyacrylamide flocculants [13]. Acrylamide may not be completely removed in many water treatment processes with some remaining after flocculation with polyacrylamides probably due to its water solubility and is not absorbed by sediment [15].
Acrylamide is evidentially a neurogenic, terratogenic or carcinogenic toxicant in animals [16]. The neurotoxic properties of acrylamide have been studied for humans in relation to occupational exposures and, experimentally, in laboratory animals. Understanding of acrylamide-induced neuropathies is quite advanced, a consequence of more than 30 years of research on the possible mechanisms of action [17]. The mechanism underlying the neurotoxic effects of acrylamide as with other toxins are interference with the kinesin-related motor proteins in nerve cells or with fusion proteins in the formation of vesicles at the nerve terminus and eventual cell death [18]. Neurotoxicity and resulting behavioral changes in acrylamide-exposed laboratory animals can reduce reproductive fitness. Further, kinesin motor proteins are important in sperm motility, which could alter reproductive parameters. Effects on kinesin proteins could also explain some of the genotoxic effects on acrylamide. These proteins form the spindle fibers in the nucleus that function in the separation of chromosomes during cell division. This could explain the clastogenic effects of the chemical noted in a number of tests for genotoxicity and assays for germ cell damage [4].
Acrylamide is a synthetic monomer with a broad spectrum of industrial applications, mainly as a precursor in the production of several polymers, such as polyacrylamide [1, 19]. High molecular weight polymers can be modified to develop nonionic, anionic, or cationic properties for specific uses [1, 20]. Various grades of acrylamide are available with the industrial grade typically with a purity of 98 to 99%. Acrylamide for laboratory use ranges from routine to pure, the former for electrophoresis, the latter for molecular applications [21]. The largest demand for acrylamide polymers in industry is for flocculation of unwanted chemical substances in water arising from mining activities, pulp and paper processing, sewage treatment, and other industrial processes. Applications are based on the principles of colloidal suspensions and used to clean up liquids, particularly aqueous media, either for disposal or human consumption [20, 22-23]. Acrylamide is also used as a chemical intermediate in the production of N-methylol acrylamide and N-butoxy acrylamide and as a superabsorbent in disposable diapers, medical, and agricultural products [24]. Small amounts of acrylamide are also used in sugar beet juice clarification, adhesives, binders for seed coatings and foundry sand, printing ink emulsion stabilizers, thickening agents for agricultural sprays, latex dispersions, textile printing paste, and water retention aids [25]. An aqueous 50% solution of acrylamide is used as acrylic copolymer dispersions in surface coatings and adhesives. In surface coatings, polymers are used as dispersants and binders to provide better pigment separation and flow. Surface coatings are used on home appliances and in the automotive trade [1, 26]. In addition, polyacrylamide has been used in both paper production process and treatment of mill wastewater [27]. Emulsions of polyacrylamide, calcium carbonate and clay are applied as a white coating in the manufacture of cardboard cartons [22]. These polymers are used as thickeners in soap and cosmetic preparations, and in skin care and hair grooming products, to impart a smooth after-feel and shine [22]. For oil drilling, liquid or powder partially-hydrolyzed polyacrylamide is used as additives to water based drilling mud to provide a lubricating film and reduce friction at the drill bit, impart stability to shale and clay and increase viscosity [1, 22, 26]. Moreover, specialized gels comprised in part of acrylamide polymers are manufactured for use as lubricants in the textile dying components to which fabric or finished garments are added. The gel lubricates the cloth preventing it from clumping together and aids pigment dispersion during the dying process to ensure an even color [22, 28]. In leather processing, acrylamide is used as polymers impart a gloss or specific feel and suppleness to leather. The hide is most commonly placed in a drum with the polymer and various other constituents such as dyes, formaldehyde and pigments, then rolled for about two hours. The polymer can also be applied by brush or spray. There is no set formulation for the components of the mix and the proportion of acrylamide polymer is at the discretion of the operator seeking to obtain the properties required in the tanned product [29-30]. Another major application of acrylamide is to reduce herbicide drift during spray applications. The polymer increases the viscosity of the herbicide solution, allowing for more uniform spray applications, and also increases plant contact time [31-33].
In worldwide usage, acrylamide is released into environment as waste during its production and in the manufacture of polyacrylamides and other polymers. Residual acrylamide concentrations in 32 polyacrylamide flocculants approved for water treatment plants ranged from 0.5 to 600 ppm [13]. Acrylamide may remain in water after treatment [15] and after flocculation with polyacrylamides due to its high solubility and is not readily adsorbed by sediment [34]. Other sources of release to water are from acrylamide-based sewer grouting and recycling of wastepaper. Another important source of contamination is from acrylonitrile-acrylamide production which releases approximately 1 g acrylamide in each liter of effluent [35]. Some reports have indicated that polyacrylamide, in the presence of sunlight and glyphosate, photolytically degrades to acrylamide monomer and this is a direct introduction of acrylamide into agricultural areas [36-38]. The half-life of acrylamide monomer in rivers ranges from weeks to months [22]. However, one report indicates that polyacrylamide does not degrade to acrylamide monomer in the presence of sunlight and glyphosate. Additionally, glyphosate appears to interact with either the acrylamide monomer or polymer, decreasing the rate of monomer degradation [39]. The most important environmental contamination results from acrylamide use in soil grouting [13]. Half-life of acrylamide in aerobic soil increases with decreasing temperature [40]. Under aerobic conditions, acrylamide was readily degraded in fresh water by bacteria with a half-life of 55-70 h, after acclimatization for 33-50 h [41]. Acrylamide has been shown to remain slightly longer in estuarine or salt than fresh water [15].
Acrylamide releases to land and water from 1987 to 1993 totaled over 18.16 tons of which about 85 percent was to water, according to Toxic Chemical Release Inventory of the U.S. Environmental Protection Agency (EPA) [40]. These releases were primarily from plastic industries which use acrylamide as a monomer. In 1992, discharges of acrylamide, reported to the Toxic Chemical Release Inventory by certain US industries included 12.71 tons to the atmosphere, 4.54 tones to surface water, 1,906.8 tones to underground injection sites, and 0.44 tones to land [4]. In an EPA study of five industrial sites that produce acrylamide and polyacrylamide, acrylamide (1.5 ppm) was found in only one sample downstream from a polyacrylamide producer and no acrylamide was detected in soil or air samples [13]. Concentrations of 0.3 ppb to 5 ppm acrylamide have been detected in terrestrial and aquatic ecosystems near industrial areas that use acrylamide and/or polyacrylamides [42-43]. Cases of human poisoning have been documented from water contaminated with acrylamide from sewer grouting. The acrylamide monomer was found to remain stable for more than 2 months in tap water [22]. Atmospheric levels around six US plants were found on an average of < 0.2 µg/m3 (0.007 ppb) in either vapor or particulate form [15]. The vapor phase chemical should react with photochemically produced hydroxyl radicals (half-life 6.6 h) and be washed out by rain [15].
The interest in environmental problems is continuously growing and there are increasing demands to seek the sustainable and controllable process which do not burden the environment significantly. Biodegradation is one of the classic methods for removal of undesired organic compounds to concentrations that are undetectable or below limits established as acceptable by regulatory agencies.
Acrylamide is likely to partially biodegrade in water within approximately 8-12 days [13]. If released on land, acrylamide can be expected to leach readily into the ground and biodegrade within a few weeks. In five surface soils that were moistened to field capacity, 74-94% degradation occurred in 14 days in three soils and 79 to 80% in 6 days in the other two soils [44]. Acrylamide may not be completely degraded in domestic sewage and water treatment facilities if residence times are relatively short [13, 45]. Further degradation through bioremediation of acrylamide to less harmful substances would alleviate environmental concerns.
Since 1982, microbial degradation of acrylamide has been explored extensively with a diversity of isolates (Table 1), mainly Bacillus, Pseudomonas and Rhodococcus [3, 46-55]. Further, numerous other microorganisms including the representatives of Arthrobacter, Xanthomonas, Rhodopseudomonas, Rastonia, Geobacillus, and a newly family of Enterobacteriaceae [49, 56-62]. Aspergillus oryzae, a filamentous fungal has also been documented as an acrylamide degrader [63].
Several acrylamide degraders use a coupling reaction of nitrile hydratase (EC 4.2.1.84) and amidase (EC 3.5.1.4) for biotransformation of acrylonitrile to acrylic acid via acrylamide as an intermediate [46, 56]. For example, R. rhodochrous J1 changed acrylonitrile to acrylamide and subsequently to acrylic acid [47] and R.\n\t\t\t\terythropolis utilized either 2-arylpropionamides or acrylamide to form acrylic acid and ammonia [64]. In China, Nocardia sp. 163, a soil derived bacterium from Taishan Mountain harboring the highest nitrile hydratase activity on acrylonitrile was also used frequently for bioconversion of acrylamide [65]. Another prominent example is Rhodococcus sp. AJ270 which is a powerful and robust nitrile hydratase/amidase-containing microorganism isolated by Guo et al [66]. An aliphatic amidase (amidohydrolase) has been found to be the responsive enzyme for the deamidation of acrylamide to acrylic acid and ammonia [50, 59, 62, 64-67].
In 1990, Shanker and his colleagues isolated an acrylamide-degrading bacterium, Pseudomonas sp., from soil using an enrichment method. This bacterium degraded high concentration of acrylamide (4 g/l) to acrylic acid and ammonia. An amidase was also found to be the relevant enzyme for the hydrolysis of acrylamide and other short chain aliphatic amides like formamide and acetamide but not on acrylamide analogues, methacrylamide and N, N-methylene bisacrylamide [48].
Many aerobic microorganisms utilize acrylamide as their sole source of carbon and energy including Pseudomonas sp. and Xanthomonas maltophilia. Nawaz and his team found amidase in cell free extracts of these species and suggested it was involved in acrylamide degradation [49]. This is consistent with their earlier conclusion of acrylamide degradation by Rhodococcus sp. [50]. Later, the denitrifying bacteria, Pseudomonas stutzeri was found to use acrylamide as substrate in the acrylonitrile–butadiene–styrene resin wastewater treatment system. The strain could remove acrylamide at concentrations below 440 mg/l under aerobic conditions [52]. Acclimation of microorganisms is believed to enhance acrylamide biodegradation. Complete degradation of acrylamide at 10–20 ppm in river water occurred in about 12 days with non-acclimated microorganisms, but in only 2 days with acclimation [3]. In 2009, scientists in Malaysia reported two acrylamide-degrading bacteria, Bacillus cereus DRY135 and Pseudomonas sp. DRYJ7. Acrylic acid was also detected as a metabolite in the degradation [53-54]. Aspergillus oryzae KBN 1010 has been the only fungi documented as an acrylamide degrader [63].
In domestic wastewater in Thailand, four novel acrylamide-degrading bacteria (Enterobacter aerogenes, Kluyvera georgiana, Klebsiella pneumoniae, and Enterococcus faecalis) were isolated. E. aerogenes and K. georgiana showed degradation potential of acrylamide up to 5000 ppm at the mesophilic temperatures and could degrade other aliphatic amides especially short to medium-chain length but not amide derivatives [60-61]. Removal of acrylamide and ammonium nitrogen from industrial wastewater by E. aerogenes was generally higher than that by mixed cultures of microorganisms [68].
\n\t\t\t\tMicroorganisms\n\t\t\t | \n\t\t\t\n\t\t\t\tSource\n\t\t\t | \n\t\t\t\n\t\t\t\tConditions\n\t\t\t | \n\t\t\t\n\t\t\t\tReference\n\t\t\t | \n\t\t
Bacteria | \n\t\t\t\n\t\t\t | \n\t\t\t | \n\t\t |
\n\t\t\t\tPseudomonas chlororaphis B23 | \n\t\t\tSoil | \n\t\t\tAerobic (Enzymatic degradation) | \n\t\t\t[46] | \n\t\t
\n\t\t\t\tArthrobacter sp. J-1 | \n\t\t\tSoil | \n\t\t\tAerobic (Enzymatic degradation) | \n\t\t\t[56] | \n\t\t
\n\t\t\t\tRhodococcus rhodochrous J1 | \n\t\t\tSoil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[47] | \n\t\t
\n\t\t\t\tPseudomonas sp. | \n\t\t\tSoil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[48] | \n\t\t
\n\t\t\t\tPseudomonas sp. \n\t\t\t\tXanthomonas maltophilia\n\t\t\t | \n\t\t\tSoil | \n\t\t\tAerobic (Immobilized cells) | \n\t\t\t[49] | \n\t\t
\n\t\t\t\tRhodococcus sp. | \n\t\t\tSoil | \n\t\t\tAerobic (Enzymatic degradation) | \n\t\t\t[50] | \n\t\t
\n\t\t\t\tRhodococcus\n\t\t\t\terythropolis MP50 | \n\t\t\tSoil | \n\t\t\tAerobic (Enzymatic degradation) | \n\t\t\t[64] | \n\t\t
\n\t\t\t\tRhodococcus sp. | \n\t\t\tSoil | \n\t\t\tAerobic (Immobilized cells) | \n\t\t\t[51] | \n\t\t
\n\t\t\t\tPseudomonas stutzeri\n\t\t\t | \n\t\t\tWastewater treatment system | \n\t\t\tAerobic (Free cells) | \n\t\t\t[52] | \n\t\t
\n\t\t\t\tRhodopseudomonas palustris\n\t\t\t | \n\t\t\tBovine slaughterhouse | \n\t\t\tPhotoheterotropic (Free cells) | \n\t\t\t[57] | \n\t\t
\n\t\t\t\tPseudomonas aeruginosa\n\t\t\t | \n\t\t\tSoil | \n\t\t\tAerobic (Free and immobilized cells) | \n\t\t\t[3] | \n\t\t
\n\t\t\t\tRalstonia eutropha TDM-3 | \n\t\t\tWastewater treatment system | \n\t\t\tAnaerobic (Free cells) | \n\t\t\t[58] | \n\t\t
\n\t\t\t\tBacillus cereus DRY135 | \n\t\t\tSoil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[53] | \n\t\t
\n\t\t\t\tPseudomonas sp. DRYJ7 | \n\t\t\tAntarctic soil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[54] | \n\t\t
Natural microbial populations | \n\t\t\tRocky Ford Highline Canal, Colorado USA | \n\t\t\tAerobic and anaerobic (Free cells) | \n\t\t\t[69] | \n\t\t
\n\t\t\t\tRalstonia eutropha AUM-01 | \n\t\t\tSoil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[59] | \n\t\t
\n\t\t\t\tEnterobacter aerogenes\n\t\t\t | \n\t\t\tDomestic wastewater | \n\t\t\tAerobic (Free and immobilized cells) | \n\t\t\t[60] | \n\t\t
Kluyvera georgianaKlebsiella pneumoniaeEnterococcus faecalis | \n\t\t\tDomestic wastewater | \n\t\t\tAerobic (Free cells) | \n\t\t\t[61] | \n\t\t
\n\t\t\t\tGeobacillus thermoglucosidasius AUT-01 | \n\t\t\tSoil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[62] | \n\t\t
\n\t\t\t\tPseudomonas aeruginosa DS-4 | \n\t\t\tSoil | \n\t\t\tAerobic (Free cells) | \n\t\t\t[55] | \n\t\t
Fungi | \n\t\t\t\n\t\t\t | \n\t\t\t | \n\t\t |
\n\t\t\t\tAspergillus oryzae KBN 1010 | \n\t\t\tFilamentous fungi used in food and beverage industries | \n\t\t\tAerobic (Free cells) | \n\t\t\t[64] | \n\t\t
Acrylamide-degrading microorganisms.
Degradation of acrylamide under anaerobic conditions has been rarely described. Recently a new strain of Rhodopseudomonas palustris was found capable of using acrylamide under photoheterotrophic conditions but grew poorly under anaerobic dark or aerobic conditions. A study of acrylamide metabolism by nuclear magnetic resonance showed the rapid deamidation of acrylamide to acrylate and further to propionate [57]. More recently, the denitrifying bacterium, Ralstonia eutropha TDM-3 isolated from the wastewater treatment system associated with the manufacture of polyacrylonitrile fiber consumed acrylamide to concentration of 1446 mg/l, above which it was toxic [58]. This report is similar with the potential of soil bacteria, Ralstonia eutropha AUM-01 and Geobacillus thermoglucosidasius AUT-01 [59, 62]. One report, and perhaps most interesting, removal of acrylamide has been found potentially with the natural microbial populations in Rocky Ford Highline Canal, Colorado USA [69]. Degradation of acrylamide occurs under aerobic or anaerobic conditions, with nitrate serving as the most favorable anaerobic electron acceptor. Phylogenetic analysis of these cosmopolitan microorganisms suggest the potential for biodegradation in similar lotic systems such as Pseudomonas, Rhodococcus, and Bacillus. New proteobacterial genera (Pectobacterium, Citrobacter, Delftia, Comomonas, and Methylobacterium) were also found [69]. Microbial degradation of a lipid in conjunction with acrylamide was also report with Pseudomonas aeruginosa DS-4. Salad oil was believed to be an essential factor for acrylamide biodegradation by this bacterium. The degradation rate of acrylamide was affected by the incubation time of the acclimated strain DS-4. Longer incubation time with acrylamide resulted in more efficient degradation [55].
Until now, we can not deny possible routes for acrylamide other than deamination via amidase [50, 59, 62, 64, 67]. The subsequent fate of acrylate is not well understood but probably involves pathways and enzymes that have been characterized to various degrees for other acrylate utilizing bacteria (Figure 1). Acrylate metabolism is believed to proceed via hydroxylation to β-hydroxypropionate, then oxidized to CO2 [48] or reduced to propionate [57]. Another plausible pathway for mineralization of acrylamide is via formation of acrylyl CoA which eliminates lactate as a final product [48].
A powerful tool that also enables unraveling acrylamide metabolic pathways is the sequential induction of catabolic enzymes and intermediatary metabolites. Further, insight into degradative pathways is also provided from assaying the probable key proteins that are synthesized at sufficient levels when acrylamide is present. Using proteome analysis, fifteen proteins differentially expressed from Enterobacter aerogenes grown on acrylamide were identified. Six protein homologues with amidohydrolase, urease accessory protein, quaternary ammonium compound resistance proteins, dipeptide transport protein, Omp36 osmoporin and large conductance mechanosensitive channel proteins (MscL) are seemingly involved in acrylamide stress response and its degradation. Five proteins identified as GroEL-like chaperonin, ArsR-transcriptional regulator, Ts- and Tu-elongation factor and trigger factor and four proteins (phosphoglycerate kinase, ATP synthase β-subunit, malate dehydrogenase and succinyl-CoA synthetase α-subunit) are expected to be relevant to adaption of E. aerogenes in the presence of acrylamide [70]. Based on the results, Charoenpanich and Tani have proposed acrylamide may be assimilated using Omp36 osmoporin and dipeptide transport proteins. Acrylamide is toxic, indeed lethal, to most microorganisms, however some bacteria have adapted their metabolism to use this substance as an energy source. Important to this adaptation is the evolution of genes that encode amidohydrolase (amidase) and other synthesis proteins that deaminate acrylamide to acrylic acid and ammonium [48, 50-51, 60-61]. With this, acrylic acid can be changed to propionate and subsequently succinyl CoA [57, 71-72] to generate energy. Potentially harmful ammonium is detoxified and with MscL protein and released from the cell [70].
Possible biological fates of acrylate produced from acrylamide deamidation.
Bioremediation is viewed as a sustainable process for wastewater treatment, which under appropriate conditions, can promote an efficient reduction of organic matter with minimal energy requirements and, therefore, low costs. Major limitations are the bioavailability of the organic matter and the finding of efficient biodegraders. Physico-chemical environmental conditions also greatly influence the rate and extent of degradation. In general, degradation efficiency is dependent on three overall factors (i) microorganisms that can degrade the specific chemical structure (ii) environmental conditions that allow the microorganisms to grow and express their degradation enzymes and (iii) good physical contact between the organic substrate and the organism.
Rapid degradation of acrylamide coupled with growth requires not only amidase or microorganism producing amidase, but also a whole pathway, i.e. a set of enzymes that are differentially synthesized in the presence of acrylamide. Although a complete catabolic pathway for acrylamide does not exist, recombination and mutation processes and exchange of genetic information between microorganisms may lead to the development of organisms with improved catabolic activities. Alternatively, microorganisms can cooperate by combining their catabolic potential in mixed cultures and in this way may completely mineralize acrylamide. Wang and Lee elucidated the effectiveness of Ralstonia eutropha TDM-3 and mixed cultures of wastewater from the manufacture of polyacrylonitrile fiber in treating acrylamide in synthetic wastewater. They found that mixed culture and R. eutropha TDM-3 can jointly consume acrylamide up to concentrations of 1446 mg/l and completely remove acrylamide with a sufficient supply of nitrate as electron acceptors [58]. A similar result has been found in E. aerogenes. If grown with mixed cultures from a municipal wastewater treatment plant, they can completely and rapidly convert acrylamide to acrylic acid [68]. Acrylamide up to 100 mg/L can efficiently be removed from amended canal water and sediment slurries under aerobic conditions. Using natural nitrate-reducing microorganisms in a canal environment, potential fate of acrylamide (70.3-85%) was found after 60 days [69].
Microorganisms typically require sufficient water, inorganic nutrients, carbon sources, and trace elements for maintenance and growth. Besides growth substrates, other specific organic compounds such as vitamins or other growth factors are essential for some microorganisms. Monosaccharides like glucose and fructose have been reported as support elements for the growth and degradation potential of acrylamide-degrading bacteria [53-54]. However, in some cases supplementation of acrylamide containing growth medium with glucose or succinate as additional carbon source demonstrated a severe repression in degrading ability [48, 71-75]. Addition of glutamate or ammonium sulfate as an additional nitrogen source to the growth medium demonstrated an increase in degradation potential compared to the cells grown only on acrylamide [48]. One interesting study found that Pseudomonas aeruginosa DS-4 isolated from lipid wastewater required salad oil for growth and acrylamide degradation [55].
Toxic compounds (e.g. heavy metals) should not be present at high concentrations, since they can inactivate essential enzymes. As explained in [51] iron (<10 mM) enhanced the rates of acrylamide degradation of Rhodococcus sp. but copper, cobalt and nickel inhibited the degradation. Mercury and chromium inhibited acrylamide degradation by Pseudomonas aeruginosa while nickel at lower concentrations (200 and 400 ppm) improved the degrading ability [3].
Optimum conditions for acrylamide biodegradation are achieved if pH and temperature are in the range of pH 6-8 and mesophilic temperature (15-30ºC), respectively [3, 45-48, 53-55]. Most microorganisms consume considerably less energy for the maintenance of basic functions under neutral conditions. This means that more energy is available for growth. It has been known that metabolic activity of tropical soils typically is high and fosters several processes such as carbohydrate fermentation and carbon dioxide production leading to the lowering of pH. Thus, for successful bioremediation of pollutants including acrylamide pH control may be essential. Addition of an inexpensive chemical such as calcium carbonate to neutralize soil pH during bioremediation can optimize remediation [76].
Studies on acrylamide biodegradation are mainly concerned with the isolation and identification of suitable microbial strains. Most studies use either free or immobilized cells for acrylamide removal. Of these, immobilized cells are advantageous because the immobilized cells are less likely than free cells to be adversely affected by predators, toxin, or parasites [77-78]. Additionally, they can be reused, saving resources and time. However, the implementation of immobilized cells may be sensitive to pH, temperature and acrylamide concentration. Moreover, large accumulations of the metabolic intermediate, acrylic acid, may affect some microbial activity [3, 51, 60]. Hence, the attempt to biotransform acrylamide with amidase or nitrile-converting enzymes via hydrolysis.
Microbial degradation of nitriles proceeds through two enzymatic pathways. Nitrilase (EC 3.5.5.1) catalyzes the direct cleavage of nitriles to the corresponding acids and ammonia, and nitrile hydratase (NHase) catalyzes the hydration of nitriles to amides. Both nitrile-converting enzymes have increasingly attracted attention as catalysts for processing many organic chemicals [79-81]. Nitrile hydratase is commonly used as the catalyst in the production of acrylamide and is known as one of the most important industrial enzymes [82-83]. Generally, the gene operon of nitrile hydratase consists of the genes for the alpha and beta subunits of NHase, the NHase activator and amidase. The amides produced by NHase are degraded to their corresponding free carboxylic acids and ammonia by the action of amidases [84]. Thus, nitrile-converting enzymes are of broad use as alternatives for acrylamide biotransformation.
Acrylic acid, the intermediate product in acrylamide catabolism, is a commodity chemical with an estimated annual production capacity of 4.2 million metric tons [85]. Acrylic acid and its esters can be used in paints, coatings, polymeric flocculants, paper and so on. It is conventionally produced from petrochemicals. Currently, most commercial acrylic acid is produced by partial oxidation of propene which produces undesirable by-products and large amount of inorganic wastes [86]. Currently, there is an innovative manufacturing method using nitrile-amide converting enzymes. For acrylamide degraders, it is initially degraded to ammonia and acrylic acid (acrylate), a process catalyzed by amidase. Then acrylate is reduced to generate energy for growth. Until now, the acrylate-utilizing enzyme has not been well characterized but believed to be acrylate reductase [48, 57]. The identification of the gene encoding this enzyme remains a challenge. Moreover, from an economic aspect, the acrylate reductase-deficient strains created by a gene-disruption method, lead to acrylic acid accumulation in wastewater and are recommended for acrylamide bioremediation in the future.
Sequence similarities have been identified using computer methods for database searches and multiple alignment, between several nitrilases, cyanide hydratase, β-alanine synthase and the first type of aliphatic amidases which hydrolyze only short-chain aliphatic amides [87]. All these enzymes involving the reduction of organic nitrogen compounds and ammonia production exhibited several conserved motifs. One of which contains an invariant cysteine that is part of the catalytic site in nitrilases. Another highly conserved motif includes an invariant glutamic acid that might also be involved in catalysis. Sequence conservation over the entire length of these enzymes, as well as the similarity in the reactions constitutes a definite family which points to a common catalytic mechanism [88]. Chemical mutagenesis and X-ray crystallography have been analyzed for three-dimensional structures of amidases. Only a few crystal structures of nitrilase-related amidases have been reported with Pseudomonas aeruginosa amidase the first [89-90]. The three dimensional-structures showed a conserved α-β-β-α sandwich fold resembling the conserved structural fold of the nitrilase superfamily structures. Analysis of the three dimension-structures identified E59, K134, and C166 as a catalytic triad [89]. Similar catalytic triad residues were also reported in the three dimensional structural models of amidase from Rhodococcus erythropolis, Helicobacter pylori, and Bacillus stearothermophilus [89] and also in the amidase of novel acrylamide-degrading Enterobacter aerogenes [91]. The crystal structure of Xanthomonas campestris XC1258 amidase showed a monomeric structure of globular α/β protein comprising mainly six α helices and two six-stranded β-sheet (Figure 2). This is the typical nitrilase-superfamily α-β-β-α fold. The hexamer preserving the eight-layered α-β-β-αα-β-β-α structure in holoenzyme across an interface has also been reported [92]. The analysis of small asymmetric catalytic site of the Geobacilus pallidus RAPc8 amidase suggested that access of a water molecule to the catalytic triad (C, E, K) side chains would be impeded by the formation of the acyl intermediate. The conserved E142 in the catalytic site acts as a general base to catalyze the hydrolysis of this intermediate [93]. This confirmed the conservation of the E, K, C catalytic triad across the nitrilase superfamily members and also supported the classification of the amidases in the nitrilase superfamily.
(a) The monomeric tertiary structure of amidase from Xanthomonas campestris XC1258, color-coded from blue (N-terminal) to red (C-terminal), and (b) the primary sequence of XC1258 amidase. Reprinted from Ref. [92].
Acrylamide amidases have similar sequences with nitrilases and seem to have descended from a common ancestry along with members of the sulfhydryl enzyme family. In these amidases an invariant cysteine residue was reported to act as the nucleophile in the catalytic mechanism and is confirmed by the three dimensional structural model of the amidase of Pseudomonas aeruginosa. This was built by comparative modeling using the crystal structure of the worm nitrilase fusion protein, NitFhit as the template. The putative catalytic triad C-E-K is conserved in all members of the nitrilase superfamily [89]. The signature amidases possesses two real active site residues D191 and S195 among the various conserved residues within the signature sequence common to all enantioselective amidases. D191N and S195A substitutions in Rhodococcus amidase has been shown to completely suppress amidase activity [94-95]. These sequences are also present within the active site sequences of aspartic proteinases. Thus, amide bond cleaving enantioselective amidases that are coupled with nitrile hydratases are evolutionary related to aspartic proteinases. Further structural characterization of the amidase produced by acrylamide-degrading bacteria should reveal what other differences are present. It may be possible to use this information to aid protein engineering of the enzymes in order to improve their efficiency and specificity.
Development of thermostable amidase is also important. Based on the three-dimensional structure of amidase, additional disulfide bridges can be engineered by site-directed mutagenesis for enzyme stabilization. Novel amidases that show broad substrate specificity may be developed to biodegrade the toxic environmental pollutants, acrylamide and amides. Random approaches such as directed evolution, reverse engineering and site-directed mutagenesis could be applied to achieve such ends.
Our understanding of the biochemistry and molecular biology of amidase is advancing rapidly and already providing information that is of use today. Moreover, recent developments in amidase studies have broadened the scope of potential applications of the enzyme in acrylamide bioremediation as well as that of acrylic acid production. I predict that these developments combined with progress in genetic engineering and enzyme crystallography will have a major effect on the practical applications of acrylamide bioremediation.
A huge demand for acrylamide as an ubiquitous monomer for industry led to its environmental presence, however the International Agency for Research on Cancer has classified this compound as a probable human carcinogen. Bioremediation seems to be the only efficient and environmentally friendly process to decompose this monomer. The first step in developing acrylamide bioremediation is to choose high potent microorganisms. Choice of microorganisms is challenging owing to the large scale degradation of acrylamide and elucidation of the intermediate in catabolic pathways is the first important step. Nevertheless, the main problem is the rapid conversion of intermediate acrylic acid to other metabolites. Research on the relationship between degradation mechanisms and membrane structure of acrylamide-utilizing bacteria awaits further characterization. It is noteworthy that successful remediation of acrylamide depends on the ability of microbes to adapt to new environmental conditions and the availability of active and stable chemical degrading bacteria. Indigenous predators, parasites and toxicants are known to severely restrict biodegradation and should be a concern.
The author is grateful to Dr. N. Kurukitkoson for his encouragement to write this review and would like to thank F.W.H. Beamish for proofreading the manuscript.
Amino acids
E: Glutamic acid
K: Lysine
C: Cysteine
D: Aspartic acid
N: Asparagine
S: Serine
A: Alanine
The advancement of nanotechnologies has made possible the development of new applications in all fields. In particular, the nanostructuring of materials has paved the way toward new concepts. Important efforts have been dedicated to metallic nanoparticles, thanks to their interesting properties in comparison to bulk materials. Specially, they are widely studied to be used for many purposes in various applications: passivation of silicon for photovoltaics [1], plasmonics [2, 3], and bionanotechnology [4]. Metallic nanoparticles are also used as catalyst for silicon nanowires’ (SiNWs) growth by top-down [5, 6] or bottom-up approaches [7]. Silicon nanowires’ properties, especially their diameter, could be tuned by controlling the metallic particles properties. In the literature, many metallic nanoparticles are reported as catalysts, such as Au [8], Ti [9], Al [10], Cu [11], Ga [12], and Pt [13]. During last years, indium is considered a very interesting catalyst because it forms a low temperature eutectic with silicon (157°C) and it induces shallow defects as it acts as a p-type dopant encouraging its use as catalyst. An important issue in SiNWs’ synthesis is the indium catalyst elaboration.
\nIndium nanoparticles could be elaborated by different techniques such as vapor deposition technique [14], electrochemical reduction [15], chemical reduction of salts [16], laser ablation [17], and reduction of indium-tin oxide or indium layers by hydrogen or helium plasma [18, 19, 20]. Iacopi et al. have obtained indium particles with diameter range of 40–80 nm by electrodeposition on silicon substrate from an aqueous solution (InCl3, KCl, and HCl) [21]. Kumar et al. have reported on the growth of indium droplets obtained with an average diameter of 90 nm by indium evaporation followed by annealing at 300°C during 5 min [22]. The obtained particles’ properties are closely related to experimental parameters such as the precursor’s concentration, the plasma flow rate, the exposition duration and the substrate temperature, or the annealing parameters.
\nIn this chapter, we report on an ex situ formation of indium particles to be used as catalyst for SiNWs’ growth using two annealing processes: a rapid thermal annealing (RTA) and a conventional process. A comparative study is carried out to investigate the annealing process effect on SiNWs’ properties. In particular, the effect of indium oxide is presented.
\nThe bottom-up approach is presented as an interesting alternative for low-cost nanowires growth. Indeed, it requires few technological steps with the possibility of SiNWs’ growth on any substrate. Several techniques have been reported, mainly chemical vapor deposition (CVD), plasma-assisted chemical vapor deposition (PECVD), laser ablation, and molecular beam epitaxy (MBE). PECVD is the technique adopted in this work. It has the same principle as the conventional CVD except that the chemical reactions will take place after the formation of plasma from the reactor gases, offering the possibility to work at low temperatures. The deposited layers’ properties strongly depend on the substrate temperature, the pressure, the growth time, the reactive gases, and the gas flow rates. The principle of SiNWs’ growth by PECVD can be resumed in four main steps:
The deposition of catalytic particles (in situ or ex situ).
The formation of a metal-silicon eutectic by supplying the particles with a precursor gas [the silane (SiH4) in the case of silicon nanowires].
Saturation of metal particle with silicon (Si), nucleation and precipitation of silicon at the substrate–metal particle interface.
The growth of SiNWs.
The SiNWs’ growth is generally explained by the vapor–liquid–solid (VLS) mode proposed by R. S. Wagner and W. C. Ellis. In this mode, the growth depends on three main elements: the precursor in its gaseous state, and the metal-silicon alloy in the liquid state, the nanowire in the solid state, and hence the nomination vapor–liquid–solid mode.
\nThe SiNWs’ growth in a PECVD reactor is carried out by following the next steps:
At Twork > T eutectic of metal-Si: the metallic particle is in its liquid state.
Introducing the precursor gas (SiH4): The silane molecules in the vapor state are adsorbed on the particle surface according to the following equation:
\n
Incorporation of Si atoms in the droplet, formation of the metal-Si alloy, and the silicon diffusion toward the alloy-substrate interface. The silicon concentration in the droplet will exceed the equilibrium concentration at the working temperature, leading to the droplet saturation and the silicon nucleation.
In the VLS mode, the catalyst surface’s properties play an important role in the SiNWs’ growth. In order to adsorb the maximum of gaseous species, the surface should be rough. For example, silane dissociation and adsorption are better on the gold-silicon (Au-Si) system’s surface than that of silicon. Indeed, the high adsorption and dissociation efficiency of silane at the Au-Si droplet permits the nanowires’ growth with a constant radius. Other parameters influence SiNWs’ growth, such as the surface tension of the catalyst droplet and the solid–liquid interface tension. The choice of the catalyst metal is very important, matching some criteria:
The eutectic temperature of the metal-silicon alloy
Vapor pressure
Silicon solubility in the metal
Technological compatibility with the current semiconductor industry
Metal diffusion in SiNWs and formation of recombination centers
Oxidation, etc.
Gold is the most commonly used metal despite silicon contamination with defects, introducing deep energy levels in the silicon bandgap. Gold, with a simple diagram phase, permits the solubility and nucleation of silicon easily at a relatively low eutectic temperature (363°C). Moreover, gold does not oxidize, increasing its catalytic activity. Gold-catalyzed SiNWs are well controlled and already integrated into prototypes such as transistors [23], biosensors [24], and photo-anodes [25].
\nSince 2001, post-transition metals like aluminum, indium, and bismuth have been studied. All these metals introduce shallow defects (dopants for silicon). Aluminum, for example, has an eutectic temperature (577°C) higher than that of gold and is very chemically reactive, especially with oxygen.
\nBismuth (Bi) is a promising catalyst. The energy level of the impurity introduced by bismuth into the silicon gap is close to the conduction band, so bismuth is an N-type dopant for silicon. Bismuth exhibits a low silicon eutectic temperature (271°C), which allows working at low growth temperatures and using flexible substrates. Despite these advantages, it is difficult to use it as SiNWs catalyst because it has a high vapor pressure, so it can evaporate easily during growth. It has a low surface tension (0.37 N/m), while gold has a higher surface tension (1.14 N/m). Unidirectional growth has been shown to be difficult with low surface tension catalysts.
\nIndium is an interesting metal to be used as catalyst. It presents a simple phase diagram with silicon (Figure 1), forming an eutectic system at 157°C, permitting low growth temperatures and flexible substrates’ use. Indium has a surface tension (0.55 N/m) higher than that of bismuth but lower than gold. However, in the presence of oxygen, indium could be oxidized, reducing thereby its catalytic behavior.
\nPhase diagram of indium-silicon system [26].
\nFigure 2 describes the silicon nanowires growth process [27]. Indium particles (In-Nps) were grown ex situ by annealing indium-coated silicon p-type (100) substrates. Indium layers of 100 nm thickness were deposited on silicon substrates by thermal evaporation. The used annealing procedures are: (1) conventional annealing with a vacuum pressure of 10−2 mbar at 600°C during 45 min, (2) RTA annealing using a home-built RTA furnace with a vacuum pressure of 10−6 mbar at different temperatures (300, 350, 400, and 450°C) during 5 min.
\nSiNWs’ growth process adopted in this work.
To synthesize SiNWs, the samples are introduced to the PECVD reactor with substrate temperature set to 400°C. Prior to precursor (SiH4) introduction, the samples are treated by hydrogen plasma during 10 min with a flow rate of 60 sccm. Then, SiH4 is introduced during 15 min with a flow rate of 10 sccm.
\nThe indium-coated silicon substrate annealed in the conventional furnace during 45 min at 600°C shows elongated and inhomogeneous islands of micrometric sizes (Figure 3). The chosen work temperature is well above the indium melting temperature (157°C), offering sufficient kinetic energy to metallic atoms to form regular particles. The observed morphology could be attributed to the presence of indium oxide. X-ray diffraction (XRD) analysis was performed to confirm these observations. In Figure 4, we compare the XRD spectra of the as-deposited indium layer and the annealed sample. The XRD patterns of the as-deposited sample show only the presence of the planes of the tetragonal crystal structure of indium. However, after annealing, the XRD spectrum shows the disappearance of indium peaks except two peaks. These peaks are replaced by peaks attributed to indium oxide planes with the presence of very intense (222) indium oxide peak. Indium oxide can explain the obtained indium particles morphology. This phenomenon is attributed to the high melting temperature (1900°C) of indium oxide compared to the chosen annealing temperature.
\n(a) SEM image of indium-coated silicon substrate annealed under conventional process. Inset: Cross-sectional SEM view of the as-deposited indium-coated silicon substrate.
XRD spectra of as-deposited indium layer and annealed sample.
So, in order to ameliorate the indium particles properties, a hydrogen plasma treatment was performed in a PECVD reactor at a substrate temperature of 400°C during 10 min, with two different flow rates of 60 and 100 sccm. XRD analysis shows the persistence of indium oxide presence after 60 sccm H2 treatment, indicating that this flow rate is not sufficient to eliminate all In2O3. When increasing hydrogen flow, In2O3 peaks have been disappeared and replaced by indium peaks (Figure 5). This result is confirmed by the SEM image of the obtained structures (Figure 6). It is noticed that the indium particles become more homogeneous and regular in size and form. Quasi-spherical particles with average size of 440 nm (Figure 6 (c)) are obtained.
\nXRD spectra of annealed layers and treated by H2 treatment with flow rates of 60 and 100 sccm.
(a-b) SEM images of indium particles obtained after conventional annealing followed by H2 treatment with flow rate of 100 sccm (c) the corresponding histogram indicating the size distribution.
H2 plasma treatment leads to the indium oxide elimination as depicted by Eq. (2) and the indium loss through evaporation leading to particles properties enhancement (density, size, and shape). Moreover, XRD results highlight the fact that the H2 plasma flow rate (100 sccm) was sufficient to eliminate all indium oxide.
\nIn this section, we have noted the indium oxide formation during the conventional annealing that is attributed to the oxygen presence. This observation is explained by the low vacuum pressure in the furnace (10−2 mbar) where the heating is mainly provided by thermal conduction. In order to eliminate the oxygen and form pure indium particles, samples must be annealed in ultra-vacuum atmosphere; however, the thermal conduction will be very slow. In this case, the annealing will occur for long durations consuming thereby much energy.
\nIn order to overcome this problem, RTA annealing based on radiation heating by infrared short waves (400–1400 nm) is used. The heating duration could be decreased, thanks to high silicon absorption in this wavelength range.
\nIndium-coated substrates were annealed at different temperatures (300, 350, 400, and 450°C) during 5 min. It is noticed in Figure 7(a) that for the temperatures 300 and 350°C, the surface morphologies are quite similar. The substrates are covered with inhomogeneous particles in size and shape, with a high surface density. An improvement in the particles shape is obtained at 400°C. At the temperature of 450°C, quasi-spherical and homogeneous particles are obtained. The structures elaborated at 450°C show an average size of 422 nm [Figure 7 (b)]. This amelioration is attributed to the indium oxide absence as confirmed by XRD (Figure 8).
\n(a) SEM image of indium particles obtained after RTA annealing; A: 300°C, B: 350°C, C: 400°C, and D: 450°C and (b) the corresponding histogram indicating the size distribution.
XRD patterns of the sample annealed at 450°C.
To study the indium oxide influence on the grown silicon nanowires, a comparative study is carried on. Silicon nanowires are grown using indium nanoparticles elaborated by the two different annealing processes: the conventional and the RTA annealing. Figure 9(a)and(b)shows the SEM images of the obtained nanowires. The elaborated indium particles have been treated by hydrogen gas with a flow rate of 60 sccm for 10 min before the silane introduction during 15 min.
\nSEM images of (a) indium particles obtained by conventional annealing and the obtained SiNWs and (b) indium particles obtained by RTA annealing and the obtained SiNWs.
As observed, the indium particles elaborated by conventional annealing morphology are enhanced and quasi-spherical particles are obtained. Despite this improvement, the SiNWs’ density is very low due to the persistence of indium oxide after the hydrogen treatment as explained in Section 3. The indium oxide forming a shell around indium is decreasing its catalytic effect. To confirm the persistence of indium oxide, XRD of the obtained SiNWs is performed (Figure 10). In addition to silicon and indium peaks, we notice the presence of In2O3 peaks explaining the obtained low density.
\nXRD spectrum of SiNWs catalyzed by indium particles elaborated by conventional annealing.
Using indium particles elaborated at 450°C by the RTA process, the SiNWs’ density is ameliorated, which is attributed to indium oxide’s absence. The quasi-totality of indium particles is active to catalyze the SiNWs’ growth.
\nIndium particles catalyzing the growth are located on the top of the silicon nanowires confirming the VLS mode. Moreover, we notice that the SiNWs’ morphology does not seem to depend on the annealing process. The obtained SiNWs in both cases are bent and kinked.
\nIn order to study the indium diffusion in the obtained SiNWs, energy dispersive spectroscopy (EDS) is performed on the top and in the middle of a silicon nanowire. Figure 11shows that the wire is consisting of silicon only indicating that indium does not diffuse in the contrary of other catalysts like gold. In addition to that, EDS performed on the catalyst particle shows that the particle is consisting of a indium-silicon alloy as explained by the VLS mode (Table 1).
\nEDS spectra of a wire performed (a) in the middle, (b) on the top, and (c) on the particle catalyst as shown in (d).
Element (atomic %) | \nParticle | \nTop of SiNW | \nMiddle of SiNW | \n
---|---|---|---|
Si | \n51.1 | \n98.8 | \n99.4 | \n
In | \n48.9 | \n1.2 | \n0.6 | \n
Atomic percentage of silicon and indium in a grown silicon wire.
Residual indium could be removed by a simple chemical method consisting of soaking samples in 5% hydrochloric acid (HCl) solution (Figure 12). The reaction between In and HCl could potentially produce two types of indium chloride: InCl2 or InCl4. Figure 13 shows the grown silicon nanowires before and after indium catalyst elimination.
\nIllustration of the experimental protocol used.
SEM images of SiNWs (a) before and (b) after catalyst elimination.
In this work, indium is used as catalyst for silicon nanowires’ growth by VLS mode using PECVD. Indium is considered as a promising metal to replace gold as it forms a low-eutectic alloy with silicon and it introduces shallow defects.
\nIndium catalyst is elaborated by annealing indium-coated silicon substrates using two different annealing processes: conventional and RTA annealing. The annealing conditions influence the catalyst morphology and as a consequence the grown SiNWs. In this work, we have shown that the indium oxide presence is affecting the growth, in particular the density.
\nThe author wants to thank Prof. Wissem Dimassi from the Laboratory of Nanomaterials and Systems for Renewable Energy (LaNSER-CRTEn-Tunisia), Prof. Kamel Khirouni from the Laboratory of Physics of Materials and Nanomaterials Applied to Environment (LaPhyMNE—University of Gabès-Tunisia), and Dr. Maroua Yaacoubi Tabassi from the Photovoltaic Laboratory (LPV-CRTEn-Tunisia) for their contributions in this work.
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\\n\\nBook: The publication as a collection of chapters compiled by IntechOpen including the Chapter. Chapter: The original literary work created by Corresponding Author and any Co-Author that is the subject of this Agreement.
\\n\\n2. CORRESPONDING AUTHOR'S GRANT OF RIGHTS
\\n\\n2.1 Subject to the following Article, the Corresponding Author grants and shall ensure that each Co-Author grants, to IntechOpen, during the full term of copyright and any extensions or renewals of that term the following:
\\n\\nThe aforementioned licenses shall survive the expiry or termination of this Agreement for any reason.
\\n\\n2.2 The Corresponding Author (on their own behalf and on behalf of any Co-Author) reserves the following rights to the Chapter but agrees not to exercise them in such a way as to adversely affect IntechOpen's ability to utilize the full benefit of this Publication Agreement: (i) reprographic rights worldwide, other than those which subsist in the typographical arrangement of the Chapter as published by IntechOpen; and (ii) public lending rights arising under the Public Lending Right Act 1979, as amended from time to time, and any similar rights arising in any part of the world.
\\n\\nThe Corresponding Author confirms that they (and any Co-Author) are and will remain a member of any applicable licensing and collecting society and any successor to that body responsible for administering royalties for the reprographic reproduction of copyright works.
\\n\\nSubject to the license granted above, copyright in the Chapter and all versions of it created during IntechOpen's editing process (including the published version) is retained by the Corresponding Author and any Co-Author.
\\n\\nSubject to the license granted above, the Corresponding Author and any Co-Author retains patent, trademark and other intellectual property rights to the Chapter.
\\n\\n2.3 All rights granted to IntechOpen in this Article are assignable, sublicensable or otherwise transferrable to third parties without the Corresponding Author's or any Co-Author’s specific approval.
\\n\\n2.4 The Corresponding Author (on their own behalf and on behalf of each Co-Author) will not assert any rights under the Copyright, Designs and Patents Act 1988 to object to derogatory treatment of the Chapter as a consequence of IntechOpen's changes to the Chapter arising from translation of it, corrections and edits for house style, removal of problematic material and other reasonable edits.
\\n\\n3. CORRESPONDING AUTHOR'S DUTIES
\\n\\n3.1 When distributing or re-publishing the Chapter, the Corresponding Author agrees to credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen. The Corresponding Author warrants that each Co-Author will also credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen, when they are distributing or re-publishing the Chapter.
\\n\\n3.2 When submitting the Chapter, the Corresponding Author agrees to:
\\n\\nThe Corresponding Author will be held responsible for the payment of the Open Access Publishing Fees.
\\n\\nAll payments shall be due 30 days from the date of the issued invoice. The Corresponding Author or the payer on the Corresponding Author's and Co-Authors' behalf will bear all banking and similar charges incurred.
\\n\\n3.3 The Corresponding Author shall obtain in writing all consents necessary for the reproduction of any material in which a third-party right exists, including quotations, photographs and illustrations, in all editions of the Chapter worldwide for the full term of the above licenses, and shall provide to IntechOpen upon request the original copies of such consents for inspection (at IntechOpen's option) or photocopies of such consents.
\\n\\nThe Corresponding Author shall obtain written informed consent for publication from people who might recognize themselves or be identified by others (e.g. from case reports or photographs).
\\n\\n3.4 The Corresponding Author and any Co-Author shall respect confidentiality rights during and after the termination of this Agreement. The information contained in all correspondence and documents as part of the publishing activity between IntechOpen and the Corresponding Author and any Co-Author are confidential and are intended only for the recipient. The contents may not be disclosed publicly and are not intended for unauthorized use or distribution. Any use, disclosure, copying, or distribution is prohibited and may be unlawful.
\\n\\n4. CORRESPONDING AUTHOR'S WARRANTY
\\n\\n4.1 The Corresponding Author represents and warrants that the Chapter does not and will not breach any applicable law or the rights of any third party and, specifically, that the Chapter contains no matter that is defamatory or that infringes any literary or proprietary rights, intellectual property rights, or any rights of privacy. The Corresponding Author warrants and represents that: (i) the Chapter is the original work of themselves and any Co-Author and is not copied wholly or substantially from any other work or material or any other source; (ii) the Chapter has not been formally published in any other peer-reviewed journal or in a book or edited collection, and is not under consideration for any such publication; (iii) they themselves and any Co-Author are qualifying persons under section 154 of the Copyright, Designs and Patents Act 1988; (iv) they themselves and any Co-Author have not assigned and will not during the term of this Publication Agreement purport to assign any of the rights granted to IntechOpen under this Publication Agreement; and (v) the rights granted by this Publication Agreement are free from any security interest, option, mortgage, charge or lien.
\\n\\nThe Corresponding Author also warrants and represents that: (i) they have the full power to enter into this Publication Agreement on their own behalf and on behalf of each Co-Author; and (ii) they have the necessary rights and/or title in and to the Chapter to grant IntechOpen, on behalf of themselves and any Co-Author, the rights and licenses expressed to be granted in this Publication Agreement. If the Chapter was prepared jointly by the Corresponding Author and any Co-Author, the Corresponding Author warrants and represents that: (i) each Co-Author agrees to the submission, license and publication of the Chapter on the terms of this Publication Agreement; and (ii) they have the authority to enter into this Publication Agreement on behalf of and bind each Co-Author. The Corresponding Author shall: (i) ensure each Co-Author complies with all relevant provisions of this Publication Agreement, including those relating to confidentiality, performance and standards, as if a party to this Publication Agreement; and (ii) remain primarily liable for all acts and/or omissions of each such Co-Author.
\\n\\nThe Corresponding Author agrees to indemnify and hold IntechOpen harmless against all liabilities, costs, expenses, damages and losses and all reasonable legal costs and expenses suffered or incurred by IntechOpen arising out of or in connection with any breach of the aforementioned representations and warranties. This indemnity shall not cover IntechOpen to the extent that a claim under it results from IntechOpen's negligence or willful misconduct.
\\n\\n4.2 Nothing in this Publication Agreement shall have the effect of excluding or limiting any liability for death or personal injury caused by negligence or any other liability that cannot be excluded or limited by applicable law.
\\n\\n5. TERMINATION
\\n\\n5.1 IntechOpen has a right to terminate this Publication Agreement for quality, program, technical or other reasons with immediate effect, including without limitation (i) if the Corresponding Author or any Co-Author commits a material breach of this Publication Agreement; (ii) if the Corresponding Author or any Co-Author (being an individual) is the subject of a bankruptcy petition, application or order; or (iii) if the Corresponding Author or any Co-Author (being a company) commences negotiations with all or any class of its creditors with a view to rescheduling any of its debts, or makes a proposal for or enters into any compromise or arrangement with any of its creditors.
\\n\\nIn case of termination, IntechOpen will notify the Corresponding Author, in writing, of the decision.
\\n\\n6. INTECHOPEN’S DUTIES AND RIGHTS
\\n\\n6.1 Unless prevented from doing so by events outside its reasonable control, IntechOpen, in its discretion, agrees to publish the Chapter attributing it to the Corresponding Author and any Co-Author.
\\n\\n6.2 IntechOpen has the right to use the Corresponding Author’s and any Co-Author’s names and likeness in connection with scientific dissemination, retrieval, archiving, web hosting and promotion and marketing of the Chapter and has the right to contact the Corresponding Author and any Co-Author until the Chapter is publicly available on any platform owned and/or operated by IntechOpen.
\\n\\n6.3 IntechOpen is granted the authority to enforce the rights from this Publication Agreement, on behalf of the Corresponding Author and any Co-Author, against third parties (for example in cases of plagiarism or copyright infringements). In respect of any such infringement or suspected infringement of the copyright in the Chapter, IntechOpen shall have absolute discretion in addressing any such infringement which is likely to affect IntechOpen's rights under this Publication Agreement, including issuing and conducting proceedings against the suspected infringer.
\\n\\n7. MISCELLANEOUS
\\n\\n7.1 Further Assurance: The Corresponding Author shall and will ensure that any relevant third party (including any Co-Author) shall, execute and deliver whatever further documents or deeds and perform such acts as IntechOpen reasonably requires from time to time for the purpose of giving IntechOpen the full benefit of the provisions of this Publication Agreement.
\\n\\n7.2 Third Party Rights: A person who is not a party to this Publication Agreement may not enforce any of its provisions under the Contracts (Rights of Third Parties) Act 1999.
\\n\\n7.3 Entire Agreement: This Publication Agreement constitutes the entire agreement between the parties in relation to its subject matter. It replaces and extinguishes all prior agreements, draft agreements, arrangements, collateral warranties, collateral contracts, statements, assurances, representations and undertakings of any nature made by or on behalf of the parties, whether oral or written, in relation to that subject matter. Each party acknowledges that in entering into this Publication Agreement it has not relied upon any oral or written statements, collateral or other warranties, assurances, representations or undertakings which were made by or on behalf of the other party in relation to the subject matter of this Publication Agreement at any time before its signature (together "Pre-Contractual Statements"), other than those which are set out in this Publication Agreement. Each party hereby waives all rights and remedies which might otherwise be available to it in relation to such Pre-Contractual Statements. Nothing in this clause shall exclude or restrict the liability of either party arising out of its pre-contract fraudulent misrepresentation or fraudulent concealment.
\\n\\n7.4 Waiver: No failure or delay by a party to exercise any right or remedy provided under this Publication Agreement or by law shall constitute a waiver of that or any other right or remedy, nor shall it preclude or restrict the further exercise of that or any other right or remedy. No single or partial exercise of such right or remedy shall preclude or restrict the further exercise of that or any other right or remedy.
\\n\\n7.5 Variation: No variation of this Publication Agreement shall be effective unless it is in writing and signed by the parties (or their duly authorized representatives).
\\n\\n7.6 Severance: If any provision or part-provision of this Publication Agreement is or becomes invalid, illegal or unenforceable, it shall be deemed modified to the minimum extent necessary to make it valid, legal and enforceable. If such modification is not possible, the relevant provision or part-provision shall be deemed deleted.
\\n\\nAny modification to or deletion of a provision or part-provision under this clause shall not affect the validity and enforceability of the rest of this Publication Agreement.
\\n\\n7.7 No partnership: Nothing in this Publication Agreement is intended to, or shall be deemed to, establish or create any partnership or joint venture or the relationship of principal and agent or employer and employee between IntechOpen and the Corresponding Author or any Co-Author, nor authorize any party to make or enter into any commitments for or on behalf of any other party.
\\n\\n7.8 Governing law: This Publication Agreement and any dispute or claim (including non-contractual disputes or claims) arising out of or in connection with it or its subject matter or formation shall be governed by and construed in accordance with the law of England and Wales. The parties submit to the exclusive jurisdiction of the English courts to settle any dispute or claim arising out of or in connection with this Publication Agreement (including any non-contractual disputes or claims).
\\n\\nLast updated: 2020-11-27
\\n\\n\\n\\n
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The Corresponding Author (acting on behalf of all Authors) and INTECHOPEN LIMITED, incorporated and registered in England and Wales with company number 11086078 and a registered office at 5 Princes Gate Court, London, United Kingdom, SW7 2QJ conclude the following Agreement regarding the publication of a Book Chapter:
\n\n1. DEFINITIONS
\n\nCorresponding Author: The Author of the Chapter who serves as a Signatory to this Agreement. The Corresponding Author acts on behalf of any other Co-Author.
\n\nCo-Author: All other Authors of the Chapter besides the Corresponding Author.
\n\nIntechOpen: IntechOpen Ltd., the Publisher of the Book.
\n\nBook: The publication as a collection of chapters compiled by IntechOpen including the Chapter. Chapter: The original literary work created by Corresponding Author and any Co-Author that is the subject of this Agreement.
\n\n2. CORRESPONDING AUTHOR'S GRANT OF RIGHTS
\n\n2.1 Subject to the following Article, the Corresponding Author grants and shall ensure that each Co-Author grants, to IntechOpen, during the full term of copyright and any extensions or renewals of that term the following:
\n\nThe aforementioned licenses shall survive the expiry or termination of this Agreement for any reason.
\n\n2.2 The Corresponding Author (on their own behalf and on behalf of any Co-Author) reserves the following rights to the Chapter but agrees not to exercise them in such a way as to adversely affect IntechOpen's ability to utilize the full benefit of this Publication Agreement: (i) reprographic rights worldwide, other than those which subsist in the typographical arrangement of the Chapter as published by IntechOpen; and (ii) public lending rights arising under the Public Lending Right Act 1979, as amended from time to time, and any similar rights arising in any part of the world.
\n\nThe Corresponding Author confirms that they (and any Co-Author) are and will remain a member of any applicable licensing and collecting society and any successor to that body responsible for administering royalties for the reprographic reproduction of copyright works.
\n\nSubject to the license granted above, copyright in the Chapter and all versions of it created during IntechOpen's editing process (including the published version) is retained by the Corresponding Author and any Co-Author.
\n\nSubject to the license granted above, the Corresponding Author and any Co-Author retains patent, trademark and other intellectual property rights to the Chapter.
\n\n2.3 All rights granted to IntechOpen in this Article are assignable, sublicensable or otherwise transferrable to third parties without the Corresponding Author's or any Co-Author’s specific approval.
\n\n2.4 The Corresponding Author (on their own behalf and on behalf of each Co-Author) will not assert any rights under the Copyright, Designs and Patents Act 1988 to object to derogatory treatment of the Chapter as a consequence of IntechOpen's changes to the Chapter arising from translation of it, corrections and edits for house style, removal of problematic material and other reasonable edits.
\n\n3. CORRESPONDING AUTHOR'S DUTIES
\n\n3.1 When distributing or re-publishing the Chapter, the Corresponding Author agrees to credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen. The Corresponding Author warrants that each Co-Author will also credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen, when they are distributing or re-publishing the Chapter.
\n\n3.2 When submitting the Chapter, the Corresponding Author agrees to:
\n\nThe Corresponding Author will be held responsible for the payment of the Open Access Publishing Fees.
\n\nAll payments shall be due 30 days from the date of the issued invoice. The Corresponding Author or the payer on the Corresponding Author's and Co-Authors' behalf will bear all banking and similar charges incurred.
\n\n3.3 The Corresponding Author shall obtain in writing all consents necessary for the reproduction of any material in which a third-party right exists, including quotations, photographs and illustrations, in all editions of the Chapter worldwide for the full term of the above licenses, and shall provide to IntechOpen upon request the original copies of such consents for inspection (at IntechOpen's option) or photocopies of such consents.
\n\nThe Corresponding Author shall obtain written informed consent for publication from people who might recognize themselves or be identified by others (e.g. from case reports or photographs).
\n\n3.4 The Corresponding Author and any Co-Author shall respect confidentiality rights during and after the termination of this Agreement. The information contained in all correspondence and documents as part of the publishing activity between IntechOpen and the Corresponding Author and any Co-Author are confidential and are intended only for the recipient. The contents may not be disclosed publicly and are not intended for unauthorized use or distribution. Any use, disclosure, copying, or distribution is prohibited and may be unlawful.
\n\n4. CORRESPONDING AUTHOR'S WARRANTY
\n\n4.1 The Corresponding Author represents and warrants that the Chapter does not and will not breach any applicable law or the rights of any third party and, specifically, that the Chapter contains no matter that is defamatory or that infringes any literary or proprietary rights, intellectual property rights, or any rights of privacy. The Corresponding Author warrants and represents that: (i) the Chapter is the original work of themselves and any Co-Author and is not copied wholly or substantially from any other work or material or any other source; (ii) the Chapter has not been formally published in any other peer-reviewed journal or in a book or edited collection, and is not under consideration for any such publication; (iii) they themselves and any Co-Author are qualifying persons under section 154 of the Copyright, Designs and Patents Act 1988; (iv) they themselves and any Co-Author have not assigned and will not during the term of this Publication Agreement purport to assign any of the rights granted to IntechOpen under this Publication Agreement; and (v) the rights granted by this Publication Agreement are free from any security interest, option, mortgage, charge or lien.
\n\nThe Corresponding Author also warrants and represents that: (i) they have the full power to enter into this Publication Agreement on their own behalf and on behalf of each Co-Author; and (ii) they have the necessary rights and/or title in and to the Chapter to grant IntechOpen, on behalf of themselves and any Co-Author, the rights and licenses expressed to be granted in this Publication Agreement. If the Chapter was prepared jointly by the Corresponding Author and any Co-Author, the Corresponding Author warrants and represents that: (i) each Co-Author agrees to the submission, license and publication of the Chapter on the terms of this Publication Agreement; and (ii) they have the authority to enter into this Publication Agreement on behalf of and bind each Co-Author. The Corresponding Author shall: (i) ensure each Co-Author complies with all relevant provisions of this Publication Agreement, including those relating to confidentiality, performance and standards, as if a party to this Publication Agreement; and (ii) remain primarily liable for all acts and/or omissions of each such Co-Author.
\n\nThe Corresponding Author agrees to indemnify and hold IntechOpen harmless against all liabilities, costs, expenses, damages and losses and all reasonable legal costs and expenses suffered or incurred by IntechOpen arising out of or in connection with any breach of the aforementioned representations and warranties. This indemnity shall not cover IntechOpen to the extent that a claim under it results from IntechOpen's negligence or willful misconduct.
\n\n4.2 Nothing in this Publication Agreement shall have the effect of excluding or limiting any liability for death or personal injury caused by negligence or any other liability that cannot be excluded or limited by applicable law.
\n\n5. TERMINATION
\n\n5.1 IntechOpen has a right to terminate this Publication Agreement for quality, program, technical or other reasons with immediate effect, including without limitation (i) if the Corresponding Author or any Co-Author commits a material breach of this Publication Agreement; (ii) if the Corresponding Author or any Co-Author (being an individual) is the subject of a bankruptcy petition, application or order; or (iii) if the Corresponding Author or any Co-Author (being a company) commences negotiations with all or any class of its creditors with a view to rescheduling any of its debts, or makes a proposal for or enters into any compromise or arrangement with any of its creditors.
\n\nIn case of termination, IntechOpen will notify the Corresponding Author, in writing, of the decision.
\n\n6. INTECHOPEN’S DUTIES AND RIGHTS
\n\n6.1 Unless prevented from doing so by events outside its reasonable control, IntechOpen, in its discretion, agrees to publish the Chapter attributing it to the Corresponding Author and any Co-Author.
\n\n6.2 IntechOpen has the right to use the Corresponding Author’s and any Co-Author’s names and likeness in connection with scientific dissemination, retrieval, archiving, web hosting and promotion and marketing of the Chapter and has the right to contact the Corresponding Author and any Co-Author until the Chapter is publicly available on any platform owned and/or operated by IntechOpen.
\n\n6.3 IntechOpen is granted the authority to enforce the rights from this Publication Agreement, on behalf of the Corresponding Author and any Co-Author, against third parties (for example in cases of plagiarism or copyright infringements). In respect of any such infringement or suspected infringement of the copyright in the Chapter, IntechOpen shall have absolute discretion in addressing any such infringement which is likely to affect IntechOpen's rights under this Publication Agreement, including issuing and conducting proceedings against the suspected infringer.
\n\n7. MISCELLANEOUS
\n\n7.1 Further Assurance: The Corresponding Author shall and will ensure that any relevant third party (including any Co-Author) shall, execute and deliver whatever further documents or deeds and perform such acts as IntechOpen reasonably requires from time to time for the purpose of giving IntechOpen the full benefit of the provisions of this Publication Agreement.
\n\n7.2 Third Party Rights: A person who is not a party to this Publication Agreement may not enforce any of its provisions under the Contracts (Rights of Third Parties) Act 1999.
\n\n7.3 Entire Agreement: This Publication Agreement constitutes the entire agreement between the parties in relation to its subject matter. It replaces and extinguishes all prior agreements, draft agreements, arrangements, collateral warranties, collateral contracts, statements, assurances, representations and undertakings of any nature made by or on behalf of the parties, whether oral or written, in relation to that subject matter. Each party acknowledges that in entering into this Publication Agreement it has not relied upon any oral or written statements, collateral or other warranties, assurances, representations or undertakings which were made by or on behalf of the other party in relation to the subject matter of this Publication Agreement at any time before its signature (together "Pre-Contractual Statements"), other than those which are set out in this Publication Agreement. Each party hereby waives all rights and remedies which might otherwise be available to it in relation to such Pre-Contractual Statements. Nothing in this clause shall exclude or restrict the liability of either party arising out of its pre-contract fraudulent misrepresentation or fraudulent concealment.
\n\n7.4 Waiver: No failure or delay by a party to exercise any right or remedy provided under this Publication Agreement or by law shall constitute a waiver of that or any other right or remedy, nor shall it preclude or restrict the further exercise of that or any other right or remedy. No single or partial exercise of such right or remedy shall preclude or restrict the further exercise of that or any other right or remedy.
\n\n7.5 Variation: No variation of this Publication Agreement shall be effective unless it is in writing and signed by the parties (or their duly authorized representatives).
\n\n7.6 Severance: If any provision or part-provision of this Publication Agreement is or becomes invalid, illegal or unenforceable, it shall be deemed modified to the minimum extent necessary to make it valid, legal and enforceable. If such modification is not possible, the relevant provision or part-provision shall be deemed deleted.
\n\nAny modification to or deletion of a provision or part-provision under this clause shall not affect the validity and enforceability of the rest of this Publication Agreement.
\n\n7.7 No partnership: Nothing in this Publication Agreement is intended to, or shall be deemed to, establish or create any partnership or joint venture or the relationship of principal and agent or employer and employee between IntechOpen and the Corresponding Author or any Co-Author, nor authorize any party to make or enter into any commitments for or on behalf of any other party.
\n\n7.8 Governing law: This Publication Agreement and any dispute or claim (including non-contractual disputes or claims) arising out of or in connection with it or its subject matter or formation shall be governed by and construed in accordance with the law of England and Wales. The parties submit to the exclusive jurisdiction of the English courts to settle any dispute or claim arising out of or in connection with this Publication Agreement (including any non-contractual disputes or claims).
\n\nLast updated: 2020-11-27
\n\n\n\n
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I am also a member of the team in charge for the supervision of Ph.D. students in the fields of development of silicon based planar waveguide sensor devices, study of inelastic electron tunnelling in planar tunnelling nanostructures for sensing applications and development of organotellurium(IV) compounds for semiconductor applications. I am a specialist in data analysis techniques and nanosurface structure. I have served as the editor for many books, been a member of the editorial board in science journals, have published many papers and hold many patents.",institutionString:null,institution:{name:"Sheffield Hallam University",country:{name:"United Kingdom"}}},{id:"54525",title:"Prof.",name:"Abdul Latif",middleName:null,surname:"Ahmad",slug:"abdul-latif-ahmad",fullName:"Abdul Latif Ahmad",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"20567",title:"Prof.",name:"Ado",middleName:null,surname:"Jorio",slug:"ado-jorio",fullName:"Ado Jorio",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Universidade Federal de Minas Gerais",country:{name:"Brazil"}}},{id:"47940",title:"Dr.",name:"Alberto",middleName:null,surname:"Mantovani",slug:"alberto-mantovani",fullName:"Alberto Mantovani",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"12392",title:"Mr.",name:"Alex",middleName:null,surname:"Lazinica",slug:"alex-lazinica",fullName:"Alex Lazinica",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/12392/images/7282_n.png",biography:"Alex Lazinica is the founder and CEO of IntechOpen. After obtaining a Master's degree in Mechanical Engineering, he continued his PhD studies in Robotics at the Vienna University of Technology. Here he worked as a robotic researcher with the university's Intelligent Manufacturing Systems Group as well as a guest researcher at various European universities, including the Swiss Federal Institute of Technology Lausanne (EPFL). During this time he published more than 20 scientific papers, gave presentations, served as a reviewer for major robotic journals and conferences and most importantly he co-founded and built the International Journal of Advanced Robotic Systems- world's first Open Access journal in the field of robotics. Starting this journal was a pivotal point in his career, since it was a pathway to founding IntechOpen - Open Access publisher focused on addressing academic researchers needs. Alex is a personification of IntechOpen key values being trusted, open and entrepreneurial. Today his focus is on defining the growth and development strategy for the company.",institutionString:null,institution:{name:"TU Wien",country:{name:"Austria"}}},{id:"19816",title:"Prof.",name:"Alexander",middleName:null,surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/19816/images/1607_n.jpg",biography:"Alexander I. Kokorin: born: 1947, Moscow; DSc., PhD; Principal Research Fellow (Research Professor) of Department of Kinetics and Catalysis, N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow.\r\nArea of research interests: physical chemistry of complex-organized molecular and nanosized systems, including polymer-metal complexes; the surface of doped oxide semiconductors. He is an expert in structural, absorptive, catalytic and photocatalytic properties, in structural organization and dynamic features of ionic liquids, in magnetic interactions between paramagnetic centers. The author or co-author of 3 books, over 200 articles and reviews in scientific journals and books. He is an actual member of the International EPR/ESR Society, European Society on Quantum Solar Energy Conversion, Moscow House of Scientists, of the Board of Moscow Physical Society.",institutionString:null,institution:{name:"Semenov Institute of Chemical Physics",country:{name:"Russia"}}},{id:"62389",title:"PhD.",name:"Ali Demir",middleName:null,surname:"Sezer",slug:"ali-demir-sezer",fullName:"Ali Demir Sezer",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/62389/images/3413_n.jpg",biography:"Dr. Ali Demir Sezer has a Ph.D. from Pharmaceutical Biotechnology at the Faculty of Pharmacy, University of Marmara (Turkey). He is the member of many Pharmaceutical Associations and acts as a reviewer of scientific journals and European projects under different research areas such as: drug delivery systems, nanotechnology and pharmaceutical biotechnology. Dr. Sezer is the author of many scientific publications in peer-reviewed journals and poster communications. Focus of his research activity is drug delivery, physico-chemical characterization and biological evaluation of biopolymers micro and nanoparticles as modified drug delivery system, and colloidal drug carriers (liposomes, nanoparticles etc.).",institutionString:null,institution:{name:"Marmara University",country:{name:"Turkey"}}},{id:"61051",title:"Prof.",name:"Andrea",middleName:null,surname:"Natale",slug:"andrea-natale",fullName:"Andrea Natale",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:null},{id:"100762",title:"Prof.",name:"Andrea",middleName:null,surname:"Natale",slug:"andrea-natale",fullName:"Andrea Natale",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"St David's Medical Center",country:{name:"United States of America"}}},{id:"107416",title:"Dr.",name:"Andrea",middleName:null,surname:"Natale",slug:"andrea-natale",fullName:"Andrea Natale",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Texas Cardiac Arrhythmia",country:{name:"United States of America"}}},{id:"64434",title:"Dr.",name:"Angkoon",middleName:null,surname:"Phinyomark",slug:"angkoon-phinyomark",fullName:"Angkoon Phinyomark",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/64434/images/2619_n.jpg",biography:"My name is Angkoon Phinyomark. I received a B.Eng. degree in Computer Engineering with First Class Honors in 2008 from Prince of Songkla University, Songkhla, Thailand, where I received a Ph.D. degree in Electrical Engineering. My research interests are primarily in the area of biomedical signal processing and classification notably EMG (electromyography signal), EOG (electrooculography signal), and EEG (electroencephalography signal), image analysis notably breast cancer analysis and optical coherence tomography, and rehabilitation engineering. I became a student member of IEEE in 2008. During October 2011-March 2012, I had worked at School of Computer Science and Electronic Engineering, University of Essex, Colchester, Essex, United Kingdom. In addition, during a B.Eng. I had been a visiting research student at Faculty of Computer Science, University of Murcia, Murcia, Spain for three months.\n\nI have published over 40 papers during 5 years in refereed journals, books, and conference proceedings in the areas of electro-physiological signals processing and classification, notably EMG and EOG signals, fractal analysis, wavelet analysis, texture analysis, feature extraction and machine learning algorithms, and assistive and rehabilitative devices. I have several computer programming language certificates, i.e. Sun Certified Programmer for the Java 2 Platform 1.4 (SCJP), Microsoft Certified Professional Developer, Web Developer (MCPD), Microsoft Certified Technology Specialist, .NET Framework 2.0 Web (MCTS). I am a Reviewer for several refereed journals and international conferences, such as IEEE Transactions on Biomedical Engineering, IEEE Transactions on Industrial Electronics, Optic Letters, Measurement Science Review, and also a member of the International Advisory Committee for 2012 IEEE Business Engineering and Industrial Applications and 2012 IEEE Symposium on Business, Engineering and Industrial Applications.",institutionString:null,institution:{name:"Joseph Fourier University",country:{name:"France"}}},{id:"55578",title:"Dr.",name:"Antonio",middleName:null,surname:"Jurado-Navas",slug:"antonio-jurado-navas",fullName:"Antonio Jurado-Navas",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/55578/images/4574_n.png",biography:"Antonio Jurado-Navas received the M.S. degree (2002) and the Ph.D. degree (2009) in Telecommunication Engineering, both from the University of Málaga (Spain). He first worked as a consultant at Vodafone-Spain. 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