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More than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\\n\\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
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\\n\\nAdditionally, each book published by IntechOpen contains original content and research findings.
\\n\\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
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Simba Information has released its Open Access Book Publishing 2020 - 2024 report and has again identified IntechOpen as the world’s largest Open Access book publisher by title count.
\n\nSimba Information is a leading provider for market intelligence and forecasts in the media and publishing industry. The report, published every year, provides an overview and financial outlook for the global professional e-book publishing market.
\n\nIntechOpen, De Gruyter, and Frontiers are the largest OA book publishers by title count, with IntechOpen coming in at first place with 5,101 OA books published, a good 1,782 titles ahead of the nearest competitor.
\n\nSince the first Open Access Book Publishing report published in 2016, IntechOpen has held the top stop each year.
\n\n\n\nMore than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\n\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\n\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\n\nAdditionally, each book published by IntechOpen contains original content and research findings.
\n\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\n\n\n\n
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In recent years, a number of new applications have also come to rely on crystallization processes such as the crystallization of nano and amorphous materials. The articles for this book have been contributed by the most respected researchers in this area and cover the frontier areas of research and developments in crystallization processes. Divided into five parts this book provides the latest research developments in many aspects of crystallization including: chiral crystallization, crystallization of nanomaterials and the crystallization of amorphous and glassy materials. 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He obtained his B.Sc in physical chemistry from Bar-Ilan University in 1989 and received his PhD from the Weizmann Institute of Science with Prof. Gary Hodes on nanomaterials synthesis (1999). He then went to the Max Planck institute of colloids and interfaces for 3 years, as postdoctoral fellow to work with Prof. M. Antonietti and Prof. H Cölfen on biomimetic chemistry and chiral polymers. In 2003 joined the staff of the chemistry department at Bar-Ilan University, where he is currently a Professor at the institute of nanotechnology at Bar-Ilan University leading the nano chirality laboratory. Prof. Mastai’s earlier interests included nanomaterials synthesis and characterization. His current research is focused on the synthesis and analysis of chiral nanosurfaces, chiral self-assembled monolayers and polymeric chiral nanoparticles. 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Circadian rhythms are well-defined biological rhythmic activities ongoing 24-h time in human metabolism. Biological cyclical variation (circadian-biological-rhythm) is a physiological and kinetic event. It is clearly known that there is a molecular and neuronal connection between circadian clock and human metabolism. Thus circadian rhythms operate almost every functions of the metabolism from sleep/wake to fasting/feeding behavior through control of the cellular and organic system [1, 2, 3]. Biological rhythm is not exclusive to human being. Almost every living organism from plant and microorganism, to animal (in other words from single cell to multicellular) has own circadian rhythm [3]. Biological rhythms provide adaptation for living organism to environment both inside and outside. Circadian rhythms are the essential component of homeostasis in human body. Biological clocks are responsible to control physiological, homeostatic, behavioral and endocrine balance in organism [4]. In a nutshell, the repetitive fluctuations in biological, physiological and biochemical functions of the organisms within the period of 24 h are called circadian rhythms. Biological clock is a physiological system, which has the capacity to measure the passage of time in the living organism. Weger et al. have been shown that how the circadian clock contributes to adult stem cell function especially in the brain and neurogenesis [5]. The main issue is to provide the organism adaptation for daily and seasonal changes [6]. Biological rhythms are responsible for secretion of the hormones, the electrical activity of the hearth, body temperature, respiratory motion, and sleep-wakefulness. The main determinative circadian rhythm of the mammalian is sleep and wakefulness cycle [7]. Circadian rhythms, which take those 24 h, are examined in two parts: as nocturnal and diurnal rhythm. Nocturnal rhythm describes changes in the biological rhythm of the night, and diurnal rhythms refer to the biological rhythms that occur during the day. Human being has a diurnal activity pattern [8]. The other classification of the circadian rhythms is the infradian and ultradian rhythms. Infradian rhythms are the long rhythms that last more than from 24 h to weeks, months (examples are lunar −29.5 days- and semi lunar −14 days- rhythm. Ultradian rhythms are the short rhythms than 24 h (examples are tidal rhythms −12 h-). Ultradian rhythms are the important part of the circadian rhythms which regulate physiological functions of the body. When circadian rhythm regulated by natural environmental conditions, it is called entrained rhythm. In the case of the regulation isolated from environment, it is named as free-running rhythm or inner rhythm. There are well-defined patterns of physiological indices such as brain wave activity, cardiovascular, respiratory function, body temperature, and circadian rhythmicity [7]. The relatively new science “chronobiology” examines this biological cyclic phenomenon in living organisms. Chronobiology investigates the underlying mechanisms of chronomes which structures timing in organisms [8, 9]. Medical chronobiology is concerned with the chronopathology and chronopharmacology. Chronophysiology, chronopathology, and chronopharmacology are defined and still developing other fields about circadian rhythm. Chronophysiology examines how fitting in time setup the transaction of organisms and biological systems. Because of circadian rhythm underlie homeostasis of the body in case of dysrhythmia, the function of individual cells and so whole organisms affects negatively [10]. It has been shown that many diseases are related to dysfunction of the circadian rhythm. Consequently, chronopathology is concerned with the effect of biological rhythm in diseases formation. It deals with the pathology of diseases caused by disrupted rhythm. Chronopharmacology search for the timing of administration of medications and effects of pharmacological agents to biological rhythm [9, 11]. It has been proved that circadian dysrhythmia has significant impact on occurring and prognosis of the many health problems [12]. For this reason, comprehending that how biological clock works could provide amelioration for obesity, metabolic diseases, mental disorders, cardiac disorders, sleep disorders, and other health problems.
\nBiological clock is a self-regulating clockwork mechanism that synchronizes oxidative and reductive cycles according to the solar cycle [13]. It provides controls of whole organism from the cell to the organ system. The main goal of circadian clock is to maintain the oscillations in a molecular level which enables light-sensitive organisms to coordinate nutrient storage and use it in accordance with the daily period of activity and rest [14]. Scientists’ key goal is to understand how such circadian oscillations could be possible. In recent years scientists has been focused on set light to molecular mechanism of circadian clocks in humans [1, 3, 4, 8, 15]. It is well known that biological clocks are composed of specific proteins (molecules) throughout the body. Almost every cell contains an autonomous molecular clock. In mammals, the main circadian clock is located within the suprachiasmatic nuclei of the hypothalamus. The master clocks (suprachiasmatic nuclei (SCN) in the human brain coordinates all these cellular clocks [16]. Approximately 100,000 neurons have been identified that cluster in the suprachiasmatic nuclei of the hypothalamus extending from bilateral nuclei just above the optic chiasma. This location provides the SCN to receive the light for keeping the cycle in time [2, 7, 17, 18, 19]. The light directly from the retina adjusts biological clock and synchronizes within a daily cycle. There are special photoreceptive ganglion cells in retina, which contain light-sensitive pigment (it is called melanopsin). The melanopsin cells are stimulated by natural daylight especially short wavelength (blue light) [18]. Exposure to natural daylight stimulates nerve pathway in SCN. Moraes et al. reported that melanopsin cells play a role in synchronizing the central circadian clock with the day. They reported that melanopsin cells convey information about ambient light to the hypothalamic suprachiasmatic nucleus [18]. Blind people also have photoreceptive cells in their eyes. Because of that, they can usually respond to daylight. The light–dark signals are transmitted through the optic nerve to the suprachiasmatic nucleus, which uses them to reset the circadian clock each day [18]. Biological clocks not only need daylight to maintain its process, but also genes that influence the circadian rhythms. Biological clocks need both light and genes to keep it on track [19]. The brain needs lights to reset itself each day and to stay on the 24-h cycle. When humans kept in continuous darkness, the body’s daily cycle tends to lengthen to about 25 h. Also people who lack genes which control the clock’s cycle have could be lengthened cycles or absent completely. Main clock allows all the tissues in the body to synchronize with each other [17, 18, 19]. It has been reported that this mechanism is implemented by feedback loops of transcription and translation of core clock proteins [17]. This is an autoregulatory transcriptional feedback mechanism. It is known that most of genomes have transcriptional regulators, which transcribed in a rhythmic manner [19]. It has been shown that circadian clocks play a key role in mitochondrial oxidative metabolism [13]. It is well known that cellular redox (oxidation and reduction) status influences the activity of clock transcription factors [13]. Peek et al. identified the clock transcription feedback loop that produces cycles of nicotinamide adenine dinucleotide (NAD+). It is known that NAD+ is an important cofactor in oxidative metabolism. NAD+-dependent deacetylase activity affects protein acetylation in mitochondria. Peek et al. have been reported that circadian control of NAD+ bioavailability modulates mitochondrial oxidative function and organismal metabolism across the 24-h fasting and feeding cycle [13]. Thus, the molecular clock makes up the fluctuations, synchronized with the environment. Essentially circadian rhythms are endogenously generated process. But they could be modulated by external stimuli. Namely it could be affected by external stimuli such as temperature (heat-cold), light (light–dark), sound, food supply, time changing travel (jet lag) and social factors (in other words social jet lag). Circadian system regulates energy metabolism of the human body. Therefore, it governs the glucose, insulin, appetite and lipid metabolism. It has been shown that cellular metabolome—the complete set of small-molecule chemicals found within a biological sample—changes according to time of the day [17]. Dopamine and melatonin are prominent hormones of the circadian biology [20]. Melatonin is the main responsible hormone for human body’s daily cycle. Melatonin receptors found a very wide distribution in the body. Suprachiasmatic nuclei control the secretion of melatonin. The primary physiological function of melatonin is to adjust light/darkness cycle in human body. Dark enables the endogenous secretion of melatonin which is constituted by the suprachiasmatic nuclei and entrained to the light/dark cycle. Light suppresses the secretion of melatonin [21]. The daily secretion of melatonin is a biochemical signal of night for preparing the organization to circadian rhythms. Melatonin secretion begins between 9 and 11 pm and peaks between 1 and 3 am. The other physiological functions of the h depend on melatonin signal. Melatonin affects cell surface receptors in central nervous system thus regulates sleep/wake cycle. Suprachiasmatic nuclei also drive the release of cortisol and growth hormone [7]. The biological rhythm of the human body could be summarized as: 00:00 Midnight, 02:00 Deepest Sleep, 04:30 Lowest Body Temperature, 06:45 Sharpest Rise in Blood Pressure, 07:30 Melatonin Secretion Stops, 08:30 Bowel Movement Likely, 09:00 Highest testosterone Secretion, 10:00 High Alertness, 12:00 Noon, 14:00 Best Coordination, 15:30 Fastest reaction time, 17:00 Greatest cardiovascular efficiency and Muscle Strength, 18:30 Highest Blood Pressure, 19:00 Highest Body Temperature, 21:00 Melatonin Secretion Starts, 22:30 Bowel Movements Suppressed [8, 10, 21]. Human physiological processes (including cerebral, renal, cardiac, hormonal and metabolic) are performed according to this cycle. As clearly seen in this cycle the human being could be arranged for feeding, sleeping, and activation time properly to their biological clocks.
\nSeveral genes have been identified in operation of biological clocks. In recent years, researchers have been focused on describing and analyzing clock gene expression [2, 15, 19]. It has been reported that one-third of all gene activity is regulated by the biological clock [2]. The circadian light receptors are encoded by the essential elements called cryptochromes (cryptochromic genes, CRY1 and CRY2). It has been accepted by the researches that cryptochromes play a fundamental role and they are the most important part of the circadian rhythm. In recent years, scientists defined myraid genes that govern circadian clocks such as BMAL1, CLOCK, CRY, PER, and TIM (specifically identified for the sleep process). It has been shown that these genes were found within the cells of nearly all body tissues but particularly active within the suprachiasmatic nuclei [22, 23]. The clock proteins which encoded by these genes in the human body could control the activity of these genes. Clock gene is the first identified gene (Vitaterna et al. 1994; Antoch et al. 1997). King et al. have identified BMAL1 gene (1997). BMAL1 gene is accepted as the heterodimeric partner of CLOCK gene. So CLOCK-BMAL1 accepted as transcriptional activator complex (Gekakis et al. 1998). Takahashi defined Period and Cryptochrome genes (Takahashi 2000). In 2002, it was defined “core circadian clock genes” (BMAL1, CLOCK, CRY1, CRY2, PER1, PER2) (Preitner et al. 2002). In the periodicity of the circadian rhythm, it has been found to be important of the regulation of the stability of the PER and CRY proteins by specific E3 ubiquitin ligase complexes [15, 22, 23, 24, 25]. All these models describe the circadian clock in mammals. Increased recognition of the responsible genes in the circadian rhythm also provides an understandable processing mechanism of the human body. It has been known that the human body possesses internal time regulators which are genetically determined. Consequently, it is well known that a genetically manifested clock in the human body governs fundamental rhythmicity and enables homeostasis of the organism. It is clearly understood that the circadian rhythmicity is responsible for physiological, biological, and biochemical integrity of the human body. However, it is still unclear that how does circadian rhythmicity integrate with the physiologic systems. Although the numerous genes have been defined in process of the biological rhythmicity, the genetic and molecular mechanisms of circadian clocks also remain unclear. Learning more about the responsible genes for circadian rhythmicity will also help us to comprehend biological patterns of the human body.
\nIn mammals, the biological clock impulse energetic cycles to maintain physiologic stability. Biological rhythms are responsible for secretion of the hormones, the electrical activity of the hearth, immunity, hearth rate, blood pressure, coagulation, body temperature, hemodynamic, respiratory motion, and sleep-wakefulness [4, 12, 17, 19]. Therefore, circadian rhythmicity enables physical and mental goodness of the human body, irregular rhythms lead to various acute (delirium, hallucination) or chronic health problems (obesity, depression) [7, 27, 28]. It has been proved that many physiological variables are related to circadian rhythm. Each cell produces building blocks of amino acids. When desirable concentration is reached, the production stops. Clock genes govern these processes. In recent years, there is growing evidence about microbiome regulates that circadian clock genes [26]. It has been identified that the murine microbiome has circadian behavior and linked it to host feeding time. Liang et al. reported that the host circadian system influences the rhythmicity of the total load and taxonomic abundances in the fecal microbiota. They have reported that disruption of the host circadian clock by deletion of BMAL1 altered the fecal microbial composition [26]. It is well known that chronic sleep restriction alone could disrupt circadian transcription [29]. Circadian dysrhythmia directly causes diseases by cellular and visceral dysfunction in the human body. Cryptochromes play a key role in the diseases caused by disrupted biological clocks. It is well known that the mutation of the cryptochrome gene completely disrupts the circadian clock. Circadian dysrhythmia causes various abnormalities via impaired major metabolic proteins which play a key role in biological clocks [30]. It has been shown that circadian rhythms were severely disrupted in hospitalized patients. Disrupted circadian rhythm affects whole system in the body from sleeping/waking to digestive systems. Studies show that disrupted circadian rhythm contributes to several diseases [27, 28, 29]. Mostly circadian dysrhythmia and metabolic disorders such as obesity and metabolic syndrome are seen together [27, 29]. It has been reported that disrupted biological clocks lead to intolerance of glucose, insulin, and lipid metabolism [27, 28, 29]. Because of the glucose homeostasis is dependent on daily light–dark cycle, in case of the desynchrony glucose regulation impaired and this situation leads to metabolic syndrome even diabetes mellitus [12, 23, 29]. In addition, it has been reported in many studies that depressive and affective disorders were accompanied by disrupted sleep–wake patterns [10, 31]. In case of circadian dysrhythmia, the normal morphology of biological rhythms are changes in one or more of the aspects of the normal cycle. This could be a change in degree of fluctuation (mostly decreased amplitude), a phase shift (mostly phase delay), or disintegration of the cycle in a chaotic pattern. It has been shown that the severity of illness was correlated with degree of circadian disruption [7]. Scientist gradually understands that variety of the diseases are rhythmic disorders [10, 28, 29, 30, 31]. The sleep disturbance is the first and overt symptoms of circadian dysrhythmia. The core temperature is one of the stable rhythms. It decreases consistently around 5 am. However, in chronic diseases fluctuates. It has been shown a correlation between severity of illness and degree of circadian disruption [7]. Cardiovascular system is a good example of organizing according to the oscillation of biological clocks. Most cardiovascular functions change with the circadian cycle. The longer-term effects of disrupted circadian rhythms are increased risk of obesity, metabolic problems, depression, mental disorders, cardiac and neurological events and even cancer. In recent years, there is a growing awareness about the negative effects of the technology to biological rhythm. Chronic exposure to artificial light causes numerous health problems from simply sleep disorders to many cancers [32]. It is known that sleep–wake disruption common in industrialized society depends on lifestyle. The main issue is how human being could keep their biological clocks in a regular system. As understood clearly in the biological cycle of human body, the daytime is optimum for food intake because of the biological rhythms peaks in the morning and afternoon [12]. Froy et al. showed that well-being could be achieved by resetting the circadian clock. They reported that timed feeding also arranges circadian rhythms [30]. In a similar way, it is obvious clearly the sleep and activation time. It is well known that there is a strong correlation between disrupted circadian rhythms and many health problems person. Based on this knowledge, scientists (consider the contrary) begun to search whether healing be guided by circadian rhythms as well. It has been shown that chronobiological interventions improved the clinical outcomes through amelioration of delirium and sleep disturbance [7, 30]. Understanding what makes biological clocks tick may provide treatments for many health problems from sleep disorders, obesity, mental health disorders, to jet lag. It can also improve ways for individuals to adjust to nighttime shift work. Learning more about the genes, which is responsible for circadian rhythms, will also help us understand biological systems and the human body.
\n\n
Human being has a diurnal activity pattern.
In a molecular level, there are thousands of biological clocks in the human body.
The main clocks in the human brain coordinate all these cellular clocks.
Biological clocks provide adaptation for living organism to environment both inside and outside.
Circadian rhythms are the essential component of homeostasis in human body.
Biological clocks are responsible for controlling physiological, homeostatic, behavioral and endocrine balance in organism.
Circadian rhythm is an autoregulatory system and drives almost every physiological, biological, and biochemical functions of the mammalians.
The main purpose of circadian rhythm is to provide the organism adaptation for daily and seasonal changes.
Chronobiology investigates the underlying mechanisms of chronomes.
Cryptochromes play a key role in the diseases caused by disrupted biological clocks.
A genetically manifested clock in the human body governs fundamental rhythmicity and enables homeostasis of the organism.
There is a molecular and neuronal connection between circadian clock and human metabolism.
Essentially circadian rhythms are endogenously generated process. But they could be modulated by external stimuli.
Chronic exposure to artificial light causes numerous health problems from simply sleep disorders to many of cancer.
The daytime is optimum for food intake because of the biological rhythms peaks in the morning and afternoon.
Disrupted circadian rhythm affects whole system in the body from sleeping/waking to digestive systems.
Understanding what makes biological clocks tick may provide treatments for many health problems from sleep disorders, obesity, mental health disorders, to jet lag.
The various chemical transformations catalyzed by enzymes make these catalysts a key goal for utilization by the promising biotechnology industries. In the recent years, intense research in the field of enzyme technology has provided numerous approaches that facilitate the practical application of enzymes. This chapter emphasizes the application of oxidoreductases which catalyze the exchange of electrons amid the donor and acceptor molecules, in reactions involving electron transfer, proton/hydrogen extraction, hydride transfer, oxygen insertion, or other imperative steps. Oxidoreductases acquire advantage from the inclusion of different cofactors - for instance heme, flavin and metal ions - to catalyze redox reactions [1]. Majority of oxidoreductases are nicotinamide cofactor-dependent enzymes which have a high preference for nicotinamide adenine dinucleotide phosphate (NADP) or nicotinamide adenine dinucleotide (NAD) and they are further classified in six major classes which are oxidases, dehydrogenases, hydroxylases, oxygenases, peroxidases and reductases [2]. This chapter demonstrates the potential applications of oxidoreductases on the growth of oxidoreductase-based diagnostic tests and better biosensors, in the design of inventive systems for crucial coenzymes regeneration, and in the formation of oxidoreductase-based approaches for synthesis of polymers and oxyfunctionalized organic substrates.
The diagnosis and monitoring of a variety of diseases is extremely demanding nowadays for routine examination of clinical samples and other associated tests. The diagnostic enzymes are used for the detection/diagnosis or prognosis of disease conditions due to their substrate specificity and quantitated activity in the presence of other proteins, and are preferred in diagnosis, which can be used as a diagnostic tool for disease detection [3]. Depending on the verity of the disease, diseased state often leads to tissue damage. In such conditions, enzymes specific to diseased organs are released into blood circulation with augmented enzyme activity. The measurement of corresponding enzyme activities in blood/plasma, or any other body fluid, has been exploited in the diagnosis of diseased tissues/organs [3].
Jixu Wang et al. [4] investigated the expression and significance of glucose-6-phosphate dehydrogenase (G6PD) in human gastric cancer progression and prognosis. Apoptosis and necrosis are two major types of cell death in normal and disease pathologies. A key signature for necrotic cells is the permeabilization of the plasma membrane which can be quantified in tissue culture settings by measuring the release of the intracellular enzyme lactate dehydrogenase (LDH). It has been described that the measuring LDH release is a useful method for the detection of necrosis [5]. Two dehydrogenases, specifically, sorbitol dehydrogenase (SDH) and LDH, are used for cancer prognosis [3]. Reports suggested that in prostate cancer [6], and precancerous colorectal neoplasms [7], an abnormal serum concentration of SDH has been observed. Additionally, an enhanced level of SDH can be observed in acute liver damage and parenchymal hepaticdiseases [3]. It has been reported that LDH, marker of anaerobic metabolism, is associated with highly invasive and metastatic breast cancer and suggested that the association of activity of LDH in tumor tissue with mammographic characteristics could help in defining aggressive breast cancers [8]. The gene expression of LDH is studied in several human malignant tumors, collectively among colorectal cancer [9], lung cancer [10, 11, 12], breast cancer [13], oral cancer [14], prostate cancer [15], germ cell cancer [16], and pancreatic cancer [17]. In recent times, the prognostic value of the serum LDH level in cancer patients has been considered as a significant area of research. Additionally, LDH performs as a prognostic marker in patients with acute leukemia [18] and sickle cell disease [19].
A biosensor is an analytical tool that comprises a biological or biologically derived sensing matter with close proximity to the physico-chemical transducer [3]. The chief function of such a device is to produce a discrete or uninterrupted signal that is comparative to the concentration of the analyte [20]. Enzyme-based chemical biosensors are based on biological recognition and in order to function, the enzymes must be accessible to catalyze a specific biochemical reaction and be stable under the normal operating circumstances of the biosensor [21]. Generally the function of oxidoreductase biosensors is dependent on charge transport amid the enzyme and an electrode surface by means of coenzymes or redox mediators [22].
Over the years, various enzyme-based biosensors have been developed, however only a few of them are commercialized. The majority of the published work on enzymatic biosensors focuses on targeted blood glucose monitoring based on amperometric techniques [3]. The earliest glucose biosensor based on glucose dehydrogenase from Erwinia sp. and carbon paste was generated by Laurinavicius et al. [23] where the enzyme was incorporated in a polylysine-albumin gel, and the anchoring material was a paste of chemically adapted carbon powder, fumed silica, and binding material. A cellulose dehydrogenase based glucose biosensor from a mutant of Corynascus thermophilus has been developed, and a glassy carbon electrode (GCE) was acquired by direct electrode position of gold nanoparticles (AuNPs). The biosensor was used for the detection of glucose in human saliva samples, with successful results in terms of both revival and association with glucose blood levels [24]. This proposes the development of noninvasive glucose monitoring devices. The details of different oxidoreductase enzymatic biosensors applied for clinical diagnosis are listed in Table 1. The first marketable biosensor (glucose biosensor) was commenced in 1975 which was derived from the electrochemical recognition of hydrogen peroxide, and the glucose oxidase was employed for the improvement of the biosensor [3]. Subsequently, Clemens et al. [25] established a novel amperometric glucose biosensor in a bedside artificial pancreas, and it was marked underneath the brand name “Biostator” by Miles (Elkhart, Indiana).
Enzymes | Analyte | Test sample | Disease diagnosed | References |
---|---|---|---|---|
Glucose oxidase | Glucose | Blood plasma, blood serum, urine, and saliva | Diabetes, hypoglycemia | [26, 27, 28, 29] |
Oxalate oxidase | Oxalate | Blood serum and urine | Idiopathic urolithiasis and various intestinal diseases | [30] |
Cholesterol oxidase | Cholesterol | Blood serum | Coronary heart disease, myocardial and cerebral infarction (stroke) | [31, 32, 33, 34] |
Lactate oxidase | Lactate | Blood plasma, blood serum, drug and biological samples | Hyper lactatemia, cardiac arrest, resuscitation, sepsis, reduced renal excretion, decreased extra hepatic metabolism, intestinal infarction and lacticacidosis | [35, 36, 37, 38, 39, 40] |
Oxidoreductase enzymatic biosensors as diagnostic tools.
The most of oxidoreductases for catabolism and anabolism significantly require two natural nicotinamide-based coenzymes (NAD and NADP), respectively. The most NAD(P)-dependent oxidoreductases choose one coenzyme as an electron acceptor or donor to the other depending on their diverse metabolic functions [41]. Generally coenzymes are involved in these oxidoreductase-catalyzed reactions to transport
Nicotinamide coenzymes based dehydrogenases are of emergent importance for the production of chiral compounds, either by reduction of a prochiral precursor or via oxidative resolution of their racemate [45]. Nevertheless, the oxidized and reduced nicotinamide cofactors regeneration is an extremely critical step as the employ of these cofactors in stoichiometric amounts is too expensive for function. There are very few enzymes which are appropriate for the regeneration of oxidized nicotinamide cofactors. Glutamate dehydrogenase can be utilized for the oxidation of NADH in addition to NADPH while l-lactate dehydrogenase is able to oxidize NADH only [45]. The reduction of NAD+ is carried out by formate and FDH [45]. Glucose-6-phosphate dehydrogenase and glucose dehydrogenase are proficient to reduce both NAD+ and NADP+ [45]. It has been reported that ADH from horse liver reduces NAD+ whereas ADHs from Lactobacillus strains catalyze the reduction of NADP+ [45]. These enzymes can be applied by their inclusion in entire cell biotransformations by an NAD(P)+-dependent major reaction to achieve in situ regeneration of the consumed cofactor [45]. And for the regeneration of the reduced cofactors NADH and NADPH numerous systems for instance engineered formate dehydrogenase [46, 47], phosphite dehydrogenase [48, 49], glucose dehydrogenase [50, 51] plus cosubstrate are well established and extensively used.
Johannes et al. [52] reported the engineering of a highly stable and active mutant phosphite dehydrogenase (12x-A176R PTDH) from Pseudomonas stutzeri and evaluation of its potential as an effective NADPH regeneration system in an enzyme membrane reactor. They have utilized two practically imperative enzymatic reactions including xylose reductase-catalyzed xylitol synthesis and alcohol dehydrogenase-catalyzed (R)-phenylethanol synthesis as models, and the mutant PTDH was compared to the commercially available NADP+-specific Pseudomonas sp. 101 formate dehydrogenase (mut Pse-FDH) that is extensively employed for NADPH regeneration [52]. Soluble water-forming NAD(P)H oxidases comprise a promising NAD(P)+ regeneration scheme since they only require oxygen as cosubstrate and produce water as only byproduct [53]. In addition, the thermodynamic equilibrium of O2 reduction is a significant driving force for mostly energetically unfavorable biocatalytic oxidations [53]. Petschacher et al. [53] presented the generation of an NAD(P)H oxidase with high activity for both cofactors, NADH and NADPH. Applicability for cofactor regeneration is shown for coupling with alcohol dehydrogenase from Sphyngobium yanoikuyae for 2-heptanone production.
Enzyme catalyzed oxidation reactions have achieved growing concern in biocatalysis recently, reflected also by numerous outstanding reviews on this topic reported in the last years [54, 55, 56]. The group of oxidoreductases, to which all enzyme catalyzing oxidoreduction reactions, comprises numerous groups of biocatalysts such as dehydrogenases, monooxygenases, dioxygenases, oxidases, peroxidases, etc. [55]. Moreover, the enzymatic oxidative polymerizations have advantages of using nontoxic catalysts and mild reaction conditions, and the specific enzyme catalysis affords regio- and chemoselective polymerizations to construct functional materials [57]. It has been reported that peroxidases with the use of hydrogen peroxide as oxidant efficiently induce the oxidative coupling of phenols to phenolic polymers, the majority of which are scarcely attained by conventional chemical catalysts [57]. In addition, it has been published that laccase and peroxidase are helpful for production of cross-linked polymers such as artificial urushi and biopolymer hydrogel [57]. Kobayashi [58] established that the enzymatic polymerization as to be an efficient method of polymer synthesis. The polymerization uses hydrolases and oxidoreductases as catalysts and this new method of polymer synthesis afforded natural polysaccharides like cellulose, amylose, xylan, and chitin, and unnatural polysaccharides catalyzed by a glycosidase from well-designed monomers, varied functionalized polyesters catalyzed by lipase from a variety of monomers, and poly-aromatics materials catalyzed by an oxidoreductase and an enzyme model complex from phenols and anilines [58]. Furthermore, vinyl polymerization has been initiated by oxidoreductase [58].
Marjanovic et al. [59] reviewed the oxidative oligomerization and polymerization of various arylamines, e.g., aniline, substituted anilines, aminonaphthalene and its derivatives, catalyzed by oxidoreductases, such as laccases and peroxidases, in aqueous, organic, and mixed aqueous organic monophasic or biphasic media. Owing to the nontoxicity of oxidoreductases and their elevated catalytic effectiveness, as well as high selectivity of enzymatic oligomerizations/polymerizations under gentle conditions by means of primarily water as a solvent and often resulting in minimal byproduct formation enzymatic oligomerizations and polymerizations of arylamines are environmentally friendly and considerably contribute to a “green” chemistry of conducting and redox-active oligomers and polymers [59].
It has been also established that oxidative enzymes comprise privileged catalysts in organic synthesis [60]. Environmentally benign reaction conditions with high selectivity are the most fascinating characteristic exhibited by these biocatalysts in contrast to classical metal-based reagents. de Gonzalo et al. [60] reviewed the new perspectives and concepts derived from oxidative enzymatic processes, involving oxidative C-C bond forming reactions, atroposelective oxidations, oxidative dynamic processes, interconnected reactions, cyclic deracemizations, oxidative desymmetrizations and artificial oxidative enzymes. Oxidoreductases comprise an imperative group of biocatalysts as they facilitate not merely the broadly used stereoselective reduction of aldehydes and ketones but also the less well exploited oxidation of alcohols and amines [53]. In addition, oxidoreductases catalyzed oxidations are utilized for production of chiral alcohols and amines by deracemization [54, 60, 61, 62]. It has been reviewed thoroughly that the oxidoreductases enable chemists to perform highly selective and efficient transformations ranging from simple alcohol oxidations to stereoselective halogenations of non-activated C-H bonds [63]. Mifsud et al. [64] demonstrated for the first time that catalytic water oxidation mediated by robust TiO2 semiconductors can be productively coupled to oxidoreductases achieving photobiocatalytic redox reactions.
One of the major applications of oxidoreductase is a pharmaceutical synthesis of 3,4-dihydroxylphenyl alanine (DOPA), which is employed in the treatment of Parkinson’s disease and the industrial process that synthesizes DOPA make use of the oxidoreductase polyphenol oxidase [65]. It has been reported that the enantioselective reduction of C-4-substituted 3,5-dixocarboxylates can be carried out by using alcohol dehydrogenase from Lactobacillus brevis (LBADH) over-expressed in E. coli [66]. Laccase can be employed to synthesize numerous complex medicinal agents including triazolo(benzo)cycloalkyl thiadiazines, vinblastine, penicillin X dimer, cephalosporin antibiotics, and dimerized vindo-line [67]. In addition laccase can be used to synthesize a range of functional organic compounds including polymers with specific mechanical/electrical/optical properties, textile dyes, cosmetic pigments, flavor agents, and pesticides [68]. Biocatalysis is facilitating technology to organic synthesis chemistry by providing high selectivity of enzymatic reactions under mild conditions makes it a very valuable tool for green chemistry.
Due to the specificity and bio-based nature, potential applications of oxidoreductases in various fields are attracting active research efforts [69]. Several products generated by oxidoreductases are finding applications as antimicrobial, detoxifying, or active personal-care agents [69]. One potential application is laccase-based in situ generation of iodine, a reagent extensively used as disinfectant [67]. It has been described that laccase-iodide salt binary iodine-generating system (for sterilization) can have several advantages over the direct iodine application [69]. Peroxidases may replace laccase for the application, even though they would require H2O2 as cosubstrate [69]. The ClO¯ and Mn(III) species formed by haloperoxidase and Mn-peroxidase are extremely effective oxidants and antimicrobial agents [70]. Peroxidase can also be used to cross-link collagen which is beneficial to the healing of damaged skin [71]. The physiological activities of lysyl oxidase comprise the extracellular matrix construction which can hasten wound-healing [72, 73]. A glucose oxidase, lactoperoxidase, and iodide system has been tested for dental care and the oxidase produces H2O2 to feed the peroxidase, so that it can produce iodine that can kill plaque-causing bacteria [74]. It has been reported that the haloperoxidase can be used to oxidatively modify rubber latex surfaces, making them less allergenic [75]. A secreted oxidoreductase may even be developed as a vaccine against secretor microbes such as, Aspergillus oryzae catalase A protein has been studied as a potential aspergillosis vaccine [69]. It has been reported that low-molecular-mass laccase purified from the mushroom Tricholoma giganteumis possesses significant HIV-1 reverse transcriptase inhibitory activity [76]. As nature’s own catalysts, enzymes acquire very diverse specificity, reactivity, and other physicochemical, catalytic, and biological properties highly enviable for miscellaneous industrial and medical applications [69].
Tremendous progress has been made in the recent years in the field of applications of oxidoreductases. Oxidoreductases metabolism is a fundamental bio-process that plays a pivotal role in all species, including humans, plants, animals, and microorganisms, as their specific function is to catalyze oxidation and reduction reactions that occur within the cell. Abnormality in this metabolic system leads to a number of metabolic disorders. Thus, owing to the remarkable properties of oxidoreductases, they can be used for the diagnosis of disorders. They can provide insight into the diseased state by diagnosis, prognosis, or by assessment of response therapy. It has been established that oxidoreductases as biosensors are becoming popular potential tools in biotechnology due to their high specificity. With oxidoreductases, the conversion of a variety of aliphatic/aromatic molecules can be achieved; inert hydrocarbons can be functionalized (by hydroxylation, sulfoxidation, epoxidation, etc.); regio-, enantio- (on racemic substrates); enantiotopo– (on prochiral sub-strates); and chemo-selective reactions can be accomplished; important synthons from inexpensive and renewable biomaterials can be constructed; and the negative environment impact can be reduced [69]. Since numerous chemical and biochemical transformations engage oxidation/reduction processes, developing practical biocatalytic applications of oxidoreductases has long been an imperative target in biotechnology.
The author gratefully acknowledges the Department of Chemistry, Goalpara College (Assam), India.
The author declares no conflict of interest.
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\\n"}]'},components:[{type:"htmlEditorComponent",content:'Copyright is the term used to describe the rights related to the publication and distribution of original Works. Most importantly from a publisher's perspective, copyright governs how Authors, publishers and the general public can use, publish, and distribute publications.
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