Dimension values of the full-scale model shown in \nFigure 6\n.
\r\n\tLiterature showed the presence of ACE2 receptors on the membrane of erythrocyte or red blood cell (RBC), indicating that erythrocyte (RBC) can be considered as a peripheral biomarker for SARS-C0V2 infection.
\r\n\r\n\tIncreased levels of glycolysis and fragmentation of RBC membrane proteins were observed in the SARS-C0V2 infected patients, demonstrating that not only RBC’s metabolism and proteome but its membrane lipidome could be influenced by SARS-C0V2 infection changing the homeostasis of the infected erythrocyte. This altered RBC may result in the clot and thrombus formation; the major signs of critically ill Covid-19 patients.
\r\n\r\n\tThis book is going to be a succinct source of knowledge not only for the specialists, researchers, academics and the students in this area but for the general public who are concern about the present situation and are interested in knowing about simple non-invasive measures for identifying viral and bacterial infections through their red blood cells.
",isbn:"978-1-83969-121-8",printIsbn:"978-1-83969-120-1",pdfIsbn:"978-1-83969-122-5",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,hash:"fa5f4b6ef59e28b6e7c1a739c57c5d2f",bookSignature:"Prof. Kaneez Fatima Shad",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/10494.jpg",keywords:"Spike Protein, Hemoglobin, Proteins for Oxygen Transport, Altered Protein Structures, RBC ACE Receptors, RBC ACE-2 Receptors, Carboxypeptidase, Mas Receptor, Metabolomics, Gas Transport, Glucose-6-Phosphate, Phosphoglycerate",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"October 15th 2020",dateEndSecondStepPublish:"November 30th 2020",dateEndThirdStepPublish:"January 29th 2021",dateEndFourthStepPublish:"April 19th 2021",dateEndFifthStepPublish:"June 18th 2021",remainingDaysToSecondStep:"2 months",secondStepPassed:!0,currentStepOfPublishingProcess:3,editedByType:null,kuFlag:!1,biosketch:"Dr. Shad is a governing body member and mentor of Women in World Neuroscience (WWN), a division of the International Brain Research Organization (IBRO). She is also a member of IBRO-APRC Global Advocacy responsible for brain research funding distribution in this region.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"31988",title:"Prof.",name:"Kaneez",middleName:null,surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad",profilePictureURL:"https://mts.intechopen.com/storage/users/31988/images/system/31988.jpg",biography:"Professor Kaneez Fatima Shad, a neuroscientist with a medical background, received Ph.D. in 1994 from the Faculty of Medicine, UNSW, Australia, followed by a post-doc at the Allegheny University of Health Sciences, Philadelphia, USA. She taught Medical and Biological Sciences in various universities in Australia, the USA, UAE, Bahrain, Pakistan, and Brunei. During this period, she was also engaged in doing research by getting local and international grants (total of over 3.3 million USD) and translating them into products such as a rapid diagnostic test for stroke and other vascular disorders. She published over 60 articles in refereed journals, edited 8 books, and wrote 7 book chapters, presented at 97 international conferences, mentored 34 postgraduate students. Set up a company Shad Diagnostics for the development of cerebrovascular handheld diagnostic tool Stroke meter into a wearable.",institutionString:"University of Technology Sydney",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"4",totalChapterViews:"0",totalEditedBooks:"6",institution:{name:"University of Technology Sydney",institutionURL:null,country:{name:"Australia"}}}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"16",title:"Medicine",slug:"medicine"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"280415",firstName:"Josip",lastName:"Knapic",middleName:null,title:"Mr.",imageUrl:"https://mts.intechopen.com/storage/users/280415/images/8050_n.jpg",email:"josip@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. From chapter submission and review, to approval and revision, copy-editing and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. I maintain constant and effective communication with authors, editors and reviewers, which allows for a level of personal support that enables contributors to fully commit and concentrate on the chapters they are writing, editing, or reviewing. I assist authors in the preparation of their full chapter submissions and track important deadlines and ensure they are met. I help to coordinate internal processes such as linguistic review, and monitor the technical aspects of the process. As an ASM I am also involved in the acquisition of editors. Whether that be identifying an exceptional author and proposing an editorship collaboration, or contacting researchers who would like the opportunity to work with IntechOpen, I establish and help manage author and editor acquisition and contact."}},relatedBooks:[{type:"book",id:"1624",title:"Patch Clamp Technique",subtitle:null,isOpenForSubmission:!1,hash:"24164a2299d5f9b1a2ef1c2169689465",slug:"patch-clamp-technique",bookSignature:"Fatima Shad Kaneez",coverURL:"https://cdn.intechopen.com/books/images_new/1624.jpg",editedByType:"Edited by",editors:[{id:"31988",title:"Prof.",name:"Kaneez",surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1359",title:"Underlying Mechanisms of Epilepsy",subtitle:null,isOpenForSubmission:!1,hash:"85f9b8dac56ce4be16a9177c366e6fa1",slug:"underlying-mechanisms-of-epilepsy",bookSignature:"Fatima Shad Kaneez",coverURL:"https://cdn.intechopen.com/books/images_new/1359.jpg",editedByType:"Edited by",editors:[{id:"31988",title:"Prof.",name:"Kaneez",surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"5780",title:"Serotonin",subtitle:"A Chemical Messenger Between All Types of Living Cells",isOpenForSubmission:!1,hash:"5fe2c461c95b4ee2d886e30b89d71723",slug:"serotonin-a-chemical-messenger-between-all-types-of-living-cells",bookSignature:"Kaneez Fatima Shad",coverURL:"https://cdn.intechopen.com/books/images_new/5780.jpg",editedByType:"Edited by",editors:[{id:"31988",title:"Prof.",name:"Kaneez",surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"6683",title:"Ion Channels in Health and Sickness",subtitle:null,isOpenForSubmission:!1,hash:"8b02f45497488912833ba5b8e7cdaae8",slug:"ion-channels-in-health-and-sickness",bookSignature:"Kaneez Fatima Shad",coverURL:"https://cdn.intechopen.com/books/images_new/6683.jpg",editedByType:"Edited by",editors:[{id:"31988",title:"Prof.",name:"Kaneez",surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"9489",title:"Neurological and Mental Disorders",subtitle:null,isOpenForSubmission:!1,hash:"3c29557d356441eccf59b262c0980d81",slug:"neurological-and-mental-disorders",bookSignature:"Kaneez Fatima Shad and Kamil Hakan Dogan",coverURL:"https://cdn.intechopen.com/books/images_new/9489.jpg",editedByType:"Edited by",editors:[{id:"31988",title:"Prof.",name:"Kaneez",surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"7842",title:"Basic and Clinical Understanding of Microcirculation",subtitle:null,isOpenForSubmission:!1,hash:"a57d5a701b51d9c8e17b1c80bc0d52e5",slug:"basic-and-clinical-understanding-of-microcirculation",bookSignature:"Kaneez Fatima Shad, Seyed Soheil Saeedi Saravi and Nazar Luqman Bilgrami",coverURL:"https://cdn.intechopen.com/books/images_new/7842.jpg",editedByType:"Edited by",editors:[{id:"31988",title:"Prof.",name:"Kaneez",surname:"Fatima Shad",slug:"kaneez-fatima-shad",fullName:"Kaneez Fatima Shad"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"6550",title:"Cohort Studies in Health Sciences",subtitle:null,isOpenForSubmission:!1,hash:"01df5aba4fff1a84b37a2fdafa809660",slug:"cohort-studies-in-health-sciences",bookSignature:"R. Mauricio Barría",coverURL:"https://cdn.intechopen.com/books/images_new/6550.jpg",editedByType:"Edited by",editors:[{id:"88861",title:"Dr.",name:"René Mauricio",surname:"Barría",slug:"rene-mauricio-barria",fullName:"René Mauricio Barría"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"1591",title:"Infrared Spectroscopy",subtitle:"Materials Science, Engineering and Technology",isOpenForSubmission:!1,hash:"99b4b7b71a8caeb693ed762b40b017f4",slug:"infrared-spectroscopy-materials-science-engineering-and-technology",bookSignature:"Theophile Theophanides",coverURL:"https://cdn.intechopen.com/books/images_new/1591.jpg",editedByType:"Edited by",editors:[{id:"37194",title:"Dr.",name:"Theophanides",surname:"Theophile",slug:"theophanides-theophile",fullName:"Theophanides Theophile"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3092",title:"Anopheles mosquitoes",subtitle:"New insights into malaria vectors",isOpenForSubmission:!1,hash:"c9e622485316d5e296288bf24d2b0d64",slug:"anopheles-mosquitoes-new-insights-into-malaria-vectors",bookSignature:"Sylvie Manguin",coverURL:"https://cdn.intechopen.com/books/images_new/3092.jpg",editedByType:"Edited by",editors:[{id:"50017",title:"Prof.",name:"Sylvie",surname:"Manguin",slug:"sylvie-manguin",fullName:"Sylvie Manguin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"3161",title:"Frontiers in Guided Wave Optics and Optoelectronics",subtitle:null,isOpenForSubmission:!1,hash:"deb44e9c99f82bbce1083abea743146c",slug:"frontiers-in-guided-wave-optics-and-optoelectronics",bookSignature:"Bishnu Pal",coverURL:"https://cdn.intechopen.com/books/images_new/3161.jpg",editedByType:"Edited by",editors:[{id:"4782",title:"Prof.",name:"Bishnu",surname:"Pal",slug:"bishnu-pal",fullName:"Bishnu Pal"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"42338",title:"Lactose and β-Glucosides Metabolism and Its Regulation in Lactococcus lactis: A Review",doi:"10.5772/50889",slug:"lactose-and-glucosides-metabolism-and-its-regulation-in-lactococcus-lactis-a-review",body:'Lactic acid bacteria (LAB) are a group of Gram-positive, non-sporulating, low-GC-content bacteria that comprise 11 bacterial genera, such as Lactococcus, Lactobacillus, Leuconostoc, Streptococcus and others (Stiles & Holzapfel, 1997). LAB have a generally regarded as safe (GRAS) Food and Drug Administration (FDA) status, and some strains of different LAB species exhibit also probiotic properties (Gilliland, 1989). They are ubiquitous in many nutrient rich environments, such as milk, meat and plant material, and some of them are permanent residents of mainly mammalian intestinal tracts, while others are able to colonize them temporarily. Due to their ability to produce lactic acid as an end product of sugar fermentation, they are industrially important and are used as starter cultures in various food-fermentation processes. The importance of LAB for humans can be appreciated from the estimated 8.5 billion kg of fermented milk produced annually in Europe, leading to human consumption of 8.5×1020 LAB (Franz et al., 2010).
Understanding the mechanisms involved in carbohydrate metabolism and its regulation in LAB is essential for improving the industrial properties of these microorganisms. There are several ways to improve the metabolic potential of LAB cells, of which metabolic engineering offers a very efficient and effective tool.
Lactococci are homofermentative, mesophilic LAB that basically inhabit two natural environments, milk and plants, of which plants seem to constitute the primary niche. Occasionally, there have been reports that L. lactis was also isolated from soil, effluent water, the skin of cattle (Klijn et al., 1995), insects (leafhoppers, termites) (Bauer et al., 2000; Latorre-Guzman et al., 1977; Schultz & Breznak, 1978) and fish (Itoi et al., 2008, 2009; Pérez et al., 2011). Adaptation of lactococcal strains from plants to the dairy environment has caused the loss of some functions, resulting in smaller chromosomes and acquisition of genes (often plasmidic) important for growth in milk (Kelly et al., 2010).
Since Lactococcus lactis was first described in 1919 (Orla-Jensen, 1919), its taxonomy has changed repeatedly and still is confusing in some aspects. This group of bacteria, previously designated lactic streptococci, was placed in the new Lactococcus taxon in 1985 (Schleifer et al., 1985). The current taxonomy of L. lactis is based on phenotype and includes four subspecies (lactis, cremoris,\n\t\t\t\t\thordniae, and the newly identified subsp. tructae) and one biovar (subsp. lactis biovar diacetylactis) (Schleifer et al., 1985; van Hylckama Vlieg et al., 2006; Pérez et al., 2011; Rademaker et al., 2007). Among them, only L. lactis subsp. hordniae and subsp. tructae have never been isolated from dairy products. The lactis and cremoris phenotypes are distinguished on the basis of several basic criteria, such as: arginine and maltose utilization, decarboxylation of glutamate to γ-aminobutyric acid (GABA), and 40°C, 4% NaCl and pH 9.2 tolerance. L. lactis subsp. cremoris strains are reported to be negative for all of these features (Nomura et al., 1999; Schleifer et al., 1985). Moreover, the biovar diacetylactis strains are able to metabolize citrate, which is converted to diacetyl, an important aroma compound. Additionally, numerous genetic studies (DNA–DNA hybridization, 16S rRNA and gene sequence analysis) of L. lactis isolates of dairy and plant origin have revealed the existence among them of two main genotypes that have also been called L. lactis subsp. lactis (lactis genotype) and L. lactis subsp. cremoris (cremoris genotype). Furthermore, it has been demonstrated that the genotype and phenotype do not always correspond within one isolate, thus introducing a degree of disorder into the taxonomy of this species (Tailliez et al., 1998). It has been observed that within the group of cremoris genotype, strains with both lactis (MG1363) and cremoris (SK11) phenotypes may occur, and, likewise, within the group of lactis genotype there are ones with lactis (KF147) as well as biovar diacetylactis (IL594) phenotypes (Bayjanov et al., 2009; Kelly et al., 2010; Nomura et al., 2002; Rademaker et al., 2007; Tanigawa et al., 2010). Hence, the L. lactis has an atypical taxonomic structure with two phenotypically distinct groups, such as L. lactis subsp. lactis and L. lactis subsp. cremoris, which may belong to two distinct genotype groups. As a result, in order to sufficiently describe the individual strains, it is necessary to specify both the genotype (cremoris or lactis) and the phenotype (cremoris, diacetylactis, or lactis).
Strains belonging to L. lactis subsp. lactis and L. lactis subsp. cremoris together with a diverse assortment of other LAB are widely used as dairy starters for the production of a vast range of fermented dairy products, including various types of cheeses, sour cream, buttermilk and butter (Daly, 1983; Davidson et al., 1996). In the dairy industry, the lactis subspecies are better for making soft cheeses and the cremoris subspecies for the hard ones. Overall, it is generally accepted that the L. lactis subsp. cremoris strains make better quality products than L. lactis subsp. lactis because of their important contribution to flavour development via their unique metabolic mechanisms (Salama et al., 1991; Sandine, 1988).
During growth in milk, the primary function of L. lactis is rapid conversion of lactose to lactic acid, which provides preservation of the fermented product by preventing growth of pathogenic and spoilage bacteria, it supports curd formation, and creates optimal conditions for ripening. Further, due to their proteolytic activity and amino acid conversion, lactococci contribute to the final texture (moisture, softness) and flavour of dairy products (Smit et al., 2005). Many of lactococcal functions vital for successful fermentations are borne on plasmids, which are a common feature in lactococci, even in strains isolated from non-dairy sources (Davidson et al., 1996). For example, specific plasmid-borne genes encode proteins involved in lactose transport and metabolism and in hydrolysis and utilization of casein (Davidson, et al., 1996; McKay, 1983). Hence, there is considerable selective pressure on dairy strains to retain these plasmids, since plasmid-cured derivatives grow poorly in milk. Since plasmids are mobile elements, they can be readily exchanged among different strains (via conjugal transfer) (Gasson, 1990).
Due to its industrial importance L. lactis has become the best studied LAB, and although most studies have been performed on a small number of laboratory strains of dairy origin, it is regarded as a model organism for this bacterial group. A number of genome sequences of L. lactis strains are available, including strains from L. lactis subsp. lactis, such as IL1403, KF147 and CV56, as well as strains from L. lactis subsp. cremoris, such as MG1363, A76, NZ9000 and SK11 (according to http://www.ncbi.nlm.nih.gov/genome/). Among them, L. lactis subsp. lactis IL1403 (Chopin et al., 1984) and L. lactis subsp. cremoris MG1363 (Gasson, 1983) are the most important laboratory strains, and they can be distinguished by differences in specific DNA sequences, including those encoding 16S rRNA (Godon et al., 1992), and by their genome organization (Le Bourgeois et al., 1995). These two strains are plasmid-cured derivatives of the dairy starter strains IL594 (IL1403) and NCDO 712 (MG1363) respectively, and due to their industrial importance, their metabolism, physiology and genetics have been extensively studied over the past years. Both belong to L. lactis subsp. lactis phenotypically, but the parent strain of IL1403 has a citrate permease plasmid (Górecki et al., 2011) and is able to metabolize citrate, placing it with L. lactis subsp. lactis biovar diacetylactis, whereas MG1363 has a lactis phenotype and a cremoris genotype (Kelly et al., 2010). Despite their physiological and 16S rRNA gene sequence similarities, they share only about 85% chromosomal sequence identity, which is comparable to the genetic distance between Escherichia coli and Salmonella typhimurium (McClelland et al., 2001; Salama et al., 1991; Wegmann et al., 2007). A derivative of MG1363 was created by the integration of the nisRK genes (involving the “NICE” system for nisin-controlled protein overexpression) into the pepN gene, yielding L. lactis NZ9000 (Kuipers et al., 1998).
Most microorganisms have adapted to growth in milk habitat due to acquisition of the ability to the use its most abundant sugar, lactose, as a carbon source. This disaccharide consists of a galactose moiety linked at its C1 via a β-galactosidic bond to the C4 of glucose. Because of the efficiency and economic importance of its fermentation, a large number of studies have focused on the utilization of lactose by LAB.
Uptake of lactose into a bacterial cell can be mediated by several pathways, such as the lactose-specific phosphotransferase system (lac-PTS), ABC protein-dependent systems and secondary system transporters like lactose-galactose antiporters and lactose-H+ symport systems (de Vos & Vaughan, 1994). While ABC protein-dependent lactose transport has been demonstrated only in non-LAB, Gram-negative Agrobacterium radiobacter (Williams et al., 1992), the lac-PTS as well as secondary lactose transport systems have been described for many LAB species.
Although LAB used as starter cultures may also convert pyruvate to a variety of end products, these pathways are not expressed during lactose fermentation, which is homolactic in most strains (Cocaign-Bousquet et al., 2002; Neves et al., 2005). Since the primary function of LAB in dairy fermentations is the conversion of lactose to lactic acid, the industrial strains are primarily selected on the basis of their ability for its rapid, homolactic fermentation (de Vos & Simons, 1988).
Starter lactococcal strains transport lactose exclusively by the most abundant in LAB uptake system for various sugars - the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). The lac-PTS has a very high affinity for this sugar and is bioenergetically the most efficient system since one lactose molecule is translocated and phosphorylated in a single step, at the expense of a single ATP equivalent. Concomitantly with transport, PTS catalyzes the phosphorylation of the incoming sugar. Phosphoenolpyruvate is the first phosphoryl donor, which phosphorylates Enzyme I (EI), and then the phosphoryl group is transferred in sequence to HPr, EIIA, EIIB, and finally, via transmembrane porter (EIIC), to the transported sugar (Lorca et al., 2010). After translocation via lac-PTS, lactose is hydrolyzed by P-β-galactosidase to glucose and galactose-6-P. While glucose enters the Embden-Meyerhof-Parnas glycolytic pathway through phosphorylation by glucokinase, galactose-6-P, before it also enters the glycolytic pathway, is further metabolized via the D-tagatose-6-P (Tag-6P) pathway. This involves three enzymes: (i) galactose-6-P isomerase (LacAB); (ii) tagatose-6-P kinase (LacC); and (iii) tagatose-1,6-diphosphate aldolase (LacD). The resulting triosephosphates (glyceraldehydes-3-P and dihydroxyacetone-P) are further metabolized via glycolysis. The operons engaged in this rapid, homolactic lactose fermentation are usually plasmid-located (lac-plasmids) and, in addition to the genes for the lac-PTS proteins and P-β-galactosidase, contain genes coding for the enzymes of the Tag-6P pathway. Their transcription is regulated by various repressors, with tagatose-6-P being the molecular inducer in L. lactis (van Rooijen et al., 1991).
It is believed that plasmid-encoded ability for rapid lactose fermentation characteristic for dairy strains was recently acquired by wild-type plant strains, as a result of their adaptation to milk-environment (Kelly et al., 2010).
Another strategy developed by LAB for lactose metabolism depends on its uptake via secondary transport systems. These systems transport lactose in an unphosphorylated form via specific permeases belonging to the LacS subfamily (TC No. 2.A.2.2.3) of the 2.A.2 glycoside-pentoside-hexuronide (GPH) family (Saier, 2000). Carriers of the LacS subgroup are chimeric in nature: at their carboxy terminal end they contain an approximately 160 amino acid hydrophilic extension homologous to the EIIA domains of PTS. Thus, lactose transport is controlled by HPr-dependent phosphorylation (Gunnewijk et al., 1999; Gunnewijk & Poolman, 2000a; Gunnewijk & Poolman, 2000b). Due to this additional domain these lactose permeases are larger than the other carriers from the GPH family, which are generally about 500 amino acids in length. Depending on the organism, LacS can mediate lactose transport coupled to proton symport or by antiport with galactose. Following its import, lactose is hydrolyzed by β-galactosidase (David et al., 1992; Vaughan et al., 1996) yielding glucose and galactose. The glucose moiety is further metabolized via glycolysis, whereas the galactose moiety follows different pathways depending on the particular LAB. While some thermophilic strains of LAB (e.g., Lactobacillus bulgaricus and Streptococcus thermophilus) are known to release the galactose moiety of lactose into the medium, other LAB (e.g., Lactobacillus helveticus, Leuconostoc lactis and Streptococcus salivarius) metabolize this saccharide via the Leloir pathway (de Vos, 1996; Poolman, 1993; Vaughan et al., 2001). This pathway was one of the first central metabolic pathways to be discovered, by L. F. Leloir and coworkers in the early 1950s. It includes the key enzyme galactokinase (GalK), and hexose-1-P uridylyltransferase (GalT) plus UDP-glucose 4-epimerase (GalE), all of which are involved in the conversion of galactose to glucose-1P. The generated glucose-1P, after conversion to glucose-6P by phosphoglucomutase, enters the glycolytic pathway. Aldose-1-epimerase, a mutarotase (GalM), is an additional, more recently characterized enzyme required for rapid galactose metabolism (Bouffard et al., 1994; Mollet & Pilloud, 1991; Poolman et al., 1990). GalM catalyses the interconversion of the α- and β-anomers of galactose. This enzyme was found to be essential for efficient lactose utilization in E. coli since cleavage of this β-galactoside by β-galactosidase yields glucose and β-D-galactose, the latter being the sole substrate for GalK (Bouffard et al., 1994).
The existence of genes encoding components of the lactose permease-β-galactosidase system seems to be limited among the L. lactis strains as they have been identified only in the genomes of the dairy-derived strain IL1403 (Bolotin et al., 2001), non-dairy NCDO2054 (Vaughan et al., 1998) and KF147 isolated from mung bean sprouts (Siezen et al., 2010). Remarkably, in addition to galactose genes of the Leloir pathway cluster, these strains contain genes needed for lactose assimilation, such as lacZ (β-galactosidase) and lacA (thiogalactoside acetyltransferase), arranged in an identical layout. Directly upstream of the aforementioned genes required for lactose hydrolysis and subsequent galactose conversion, there is the gene encoding the LacS permease for sugar uptake.
Some details concerning the role of the lactose permease-β-galactosidase system in lactose utilization have been reported for the slow lactose fermenter - L. lactis NCDO2054 (Vaughan et al., 1998), and for the devoid of the lac-plasmid, essentially lactose-negative L. lactis IL1403 strain (starts to utilize lactose slowly after approximately 40 h of incubation) (Aleksandrzak-Piekarczyk et al., 2005). Since these strains possess the complete lactose permease-β-galactosidase system and an active Leloir pathway, it seems odd that they are barely capable of lactose metabolism. In the case of L. lactis NCDO2054, which can accumulate a high intracellular concentration of lactose-6-phosphate by using an efficient lac-PTS and possesses low-level P-β-galactosidase activity, it has been suggested that the slow fermentation of lactose may be due to this rate-limiting P-β-galactosidase activity and the inhibitory effect of the accumulated lactose-6-phosphate (Bissette & Anderson 1974; Crow & Thomas, 1984). However, other explanations of lactose fermentation problem can be envisaged: (i) lactose transport is inefficient due to low affinity of LacS for lactose or (ii) the strains lack a functional β-galactosidase. Indeed, the lacS gene of L. lactis IL1403 is almost identical to that of L. lactis NCDO2054, but also to galP of the lactose-negative L. lactis MG1363 strain (Grossiord et al., 2003). These permeases belong to the same subfamily (TC No. 2.A.2.2.3 according to the Transporter Classification Database: http://www.tcdb.org/; Saier, 2000), which includes transporters specific for galactose uptake, in contrast to LacS permeases of another subfamily (TC No. 2.A.2.2.1) with a proven high lactose-transport rate. The lack of LacS involvement in lactose transport is confirmed by the fact that disruption of lacS in L. lactis IL1403 had a minor effect on lactose assimilation (Aleksandrzak-Piekarczyk et al., 2005). Another indispensable factor in lactose assimilation, the β-galactosidase enzyme, is also encoded by the genomes of L. lactis IL1403 and NCDO2054 strains. In spite of the high similarity in the protein level of both enzymes, β-galactosidase of L. lactis NCDO2054, in contrast to the one of L. lactis IL1403 (Aleksandrzak-Piekarczyk et al., 2005), seems to be highly active and strongly regulated (Griffin et al., 1996). It has been suggested that the lacZ gene of L. lactis IL1403 may not be expressed or the encoded enzyme may be inactive since this strain does not exhibit β-galactosidase activity (Aleksandrzak-Piekarczyk et al., 2005). Furthermore, the in trans complementation of chromosomal lacZ by an active β-galactosidase in L. lactis IL1403 did not improve its ability for lactose assimilation, indicating that the lack of β-galactosidase activity is not the only obstacle in its ability to efficiently ferment lactose (unpublished personal observations).
Taken together, it seems that in L. lactis strains lactose permease-β-galactosidase systems play a minor role in lactose assimilation or function under certain environmental conditions. It appears that the major obstacle is the galactose-specific LacS permease, which shows only weak affinity for lactose and functions almost only in transport of galactose (Fig. 1). This thesis is confirmed by the study of Solem et al. (2008), in which an efficient lactose transporter (LacS; TC No. 2.A.2.2.1 ) and β-galactosidase (LacZ), encoded by the lacSZ operon, were introduced from lactose-positive S. thermophilus into the lactose-negative strain L. lactis MG1363, devoid of lactose permease-β-galactosidase system. As a result, fast-growing lactose-positive mutant strains were obtained. This shows that addition of the LacSZ system containing LacS with a proven high lactose-transport rate can strongly increase the lactose-transport capacity in L. lactis.
In addition to dairy environment, plant surfaces and fermenting plant material are also important ecosystems occupied by L. lactis. With regard to fermentation, lactococcal strains usually occur there only at the beginning of this process, to be later replaced by microorganisms more resistant to low pH values (Kelly & Ward, 2002; Kelly et al., 1998). The majority of plant-associated strains belong to L. lactis subsp. lactis, whereas L. lactis subsp. cremoris is typical for dairy fermentations (Kelly & Ward, 2002; Kelly et al., 1998). In comparison to the dairy environment, fermenting plant material differs highly with respect to chemical composition, exhibiting, for instance, much lower protein concentration and wider availability of carbohydrates other than lactose. The ability of plant-associated L. lactis subsp. lactis strains to utilize such a large variety of plant carbohydrates is reflected in their genomes and sugar fermentation capabilities. Comparison between milk- and plant-associated lactococcal strains clearly shows that the latter possess a larger number of genes involved in transport and metabolism of carbohydrates, resulting in their increased sugar fermentation capabilities (Siezen et al., 2008).
Besides lactose, the PTS systems can also transport various other carbohydrates, including sugars widely distributed in plants, namely β-glucosides, like e.g. amygdalin, arbutin, cellobiose, esculin, gentobiose and salicin (Tobisch et al., 1997). Except for amygdalin, these sugars are composed of two molecules joined by the β-glucosidic bond, of which at least one is glucose. The best known example of this group is cellobiose, the structural unit of one of the most abundant renewable polymers on earth – cellulose, and also the main product in its enzymatic hydrolysis (Teeri, 1997). Unlike most of other β-glucosides (aryl-β-glucosides e.g., arbutin, amygdalin, esculin, and salicin), which are composed of a single glucose molecule and respective aglycone, cellobiose consists of two glucose molecules linked via a β(1-4) bond.
It is well known from sugar fermentation characteristics that L. lactis strains of different origin can utilize a variety of β-glucosides (e.g., Aleksandrzak-Piekarczyk et al., 2011; Bardowski et al., 1995; Fernández et al., 2011; Siezen et al., 2008). The metabolic potential for catabolism of these sugars can be chromosomally encoded by more than one genetic system, as was shown for L. lactis IL1403. Eight genes, which encode proteins homologous to EII proteins of β-glucoside-dependent PTS, involved in the uptake and phosphorylation of β-glucosides have been found throughout the L. lactis IL1403 chromosome (Bolotin et al., 2001). Three of them encode the three-domain EIIABC PTS components (PtbA, YedF and YleE), another three, EIIC permeases (CelB, PtcC and YidB), one an EIIA component (PtcA) and one an EIIB component (PtcB). CelB, PtcA, PtcB, PtcC and YidB are members of the Lac family (TC No. 4.A.3), which includes several lactose porters of Gram-positive bacteria as well as the E. coli and Borrelia burgdorferi N,N\'-diacetylchitobiose (Chb) porters (according to http://www.tcdb.org/). The involvement of CelB and CelB/PtcC permeases in cellobiose transport has been experimentally confirmed in L. lactis IL1403 and MG1363, respectively (Aleksandrzak-Piekarczyk et al., 2011; Campelo et al., 2011). Although L. lactis IL1403 has such a large number of β-glucosides-specific PTS systems, CelB is the only permease operative in cellobiose uptake in this strain (Aleksandrzak-Piekarczyk et al., 2011) (Fig. 1), whereas in L. lactis MG1363 also another PTS permease, namely PtcC, seems to participate in the transport of this sugar, albeit to a much lesser extent than CelB (Campelo et al., 2011). It has been proposed that the observed low expression of the ptcC gene may be the result of repression by carbon catabolite control protein A (CcpA) as mutations in its binding site (catabolite responsive element - cre) in the ptcC promoter region led to high upregulation of this gene in strain NZ9000 compared to strain MG1363, even under repressive conditions (Linares et al., 2010).
On the other hand, the EIIAB components, namely PtcA and PtcB, seem to be more versatile, being involved in the metabolism of numerous sugars (arbutin, cellobiose, glucose, lactose, salicin) in L. lactis (Aleksandrzak-Piekarczyk et al., 2011; Castro et al., 2009; Pool et al., 2006). No other PTS systems dedicated to transport of other β-glucosides have yet been described in detail in any L. lactis strain. However, according to unpublished preliminary data, the PtbA protein appears to be involved in the transport of arbutin, esculin and salicin, but not cellobiose, in L. lactis IL1403 (unpublished personal observation) (Fig. 1). In this strain, inactivation of the ptbA gene led to serious defects in growth in medium supplemented with each of these sugars (unpublished).
After translocation by PTS through the bacterial membrane, the P-β-glucoside sugar is cleaved by P-β-glucosidase into glucose and glucose-6P or the respective aglycon (Tobisch et al., 1997). There are plenty of genes encoding P-β-glucosidases present in L. lactis chromosomes sequenced so far. Their large number is probably the result of adaptation of these bacteria to life on plants with abundant where β-glucosides. However, the data concerning their involvement in β-glucosides assimilation are rather scarce in scientific literature. It has only been demonstrated that a P-β-glucosidase, BglS, is responsible for hydrolysis of cellobiose, but not of salicin in L. lactis IL1403 (Aleksandrzak-Piekarczyk et al., 2005) (Fig. 1). On the other hand, no function has been attributed to another P-β-glucosidase encoded by the bglA gene, and forming one operon with ptcC. According to unpublished results, the disruption of bglA did not alter growth of the IL1403 mutant strain in medium supplemented with a wide array of sugars (unpublished personal analysis).
Expression of β-glucosides’ catabolic genes can be controlled by various regulatory mechanisms. Among them, catabolite repression (Aleksandrzak-Piekarczyk et al., 2005, 2011; Zomer at al., 2007) and transcriptional antitermination through the BglR protein (Bardowski et al., 1994) were shown to be operational in L. lactis. The antitermination mechanism allows for expression of β-glucoside-specific genes in the absence of a metabolically preferred carbon source, such as glucose (Rutberg, 1997). It is believed that antiterminator proteins act by binding to a ribonucleic antiterminator (RAT) site at a specific mRNA secondary structure to prevent the formation of a hairpin terminator structure that would otherwise terminate transcription (Aymerich & Steinmetz, 1992; Rutberg, 1997). The binding of the antiterminator protein to the mRNA permits transcription through the sequestered terminator sequence into a β-glucoside-specific operon that is not normally transcribed. The function of BglR has been studied earlier in L. lactis IL1403, and it was shown to be involved in the activation of assimilation of β-glucosides such as arbutin, esculin and salicin, except for cellobiose (Bardowski et al., 1994; 1995) (Fig. 1). Inspection of the L. lactis IL1403 genome sequence downstream of bglR revealed the presence of two genes, ptbA and bglH, encoding proteins homologous to a putative three-domain EIIABC PTS component specific for the assimilation of β-glucosides, and P-β-glucosidase, respectively. Upstream of bglR, a putative cre-box (differing from the cre consensus by one nucleotide), a putative promoter sequence and a RAT sequence were identified. This RAT sequence has been reported previously (Bardowski et al., 1994, 1995) to be involved in the autoregulation of BglR. This sequence partially overlapped a putative rho-independent terminator, which comprised six nucleotides at the 3’ end of the RAT. The ptbA gene is located 141 nt downstream of bglR. In silico sequence analysis revealed that the ptbA gene is also preceded by a DNA sequence highly similar to the RAT consensus sequence, suggesting that the regulation of ptbA expression may involve the BglR-mediated antitermination mechanism (unpublished personal analysis). Moreover, the short intergenic DNA region (47 nt) between ptbA and the next gene (bglH), plus the lack of an obvious hairpin structure or a promoter sequence strongly suggest that these two genes might be cotranscribed, and thus undergo common BglR-mediated regulation (unpublished) (Fig. 1).
The existence in several lactococcal strains devoid of lac-plasmids of cryptic lactose transport and catabolism systems has already been suggested in earlier studies (Anderson & McKay, 1977; Cords & McKay, 1974; de Vos & Simons, 1988; Simons et al., 1993). The presence in L. lactis of chromosomally-encoded lactose permease has been proposed since introduction of the E. coli\n\t\t\t\tlacZ gene into a lactose-deficient L. lactis strain restored its ability to utilize lactose (de Vos & Simons, 1988). Moreover, P-β-galactosidase activities have also been detected in strains cured of their lactose plasmids, suggesting the presence of chromosomally-encoded cryptic lac-PTS(s) (Anderson & McKay, 1977; Cords & McKay, 1974). However, it was suggested that these PTSs are not specific for lactose, but rather for the translocation of other sugars (e.g., β-glucosides), and lactose could be transported alternatively. This hypothesis was supported by observations suggesting that a putative P-β-glucosidase, involved in cellobiose hydrolysis, is probably also involved in lactose-6-P cleavage in L. lactis strain ATCC7962 (Simons et al., 1993). This seems reasonable, as according to http://www.tcdb.org/, PTS lactose transporters belong to the Lac family (TC No. 4.A.3) and porters of this family have broad substrate specificity. Besides lactose, they can also transport aromatic β-glucosides and cellobiose.
Until recently (Aleksandrzak et al., 2000; Aleksandrzak-Piekarczyk et al., 2005, 2011; Kowalczyk et al., 2008), little information on the organization in L. lactis strains of chromosomal alternative lactose utilization genes has been available. It was shown that in lac-plasmid-free, and thus lactose-negative L. lactis IL1403, the ability to assimilate lactose can be induced in two ways: (i) by the presence of cellobiose or (ii) by inactivation of CcpA (Aleksandrzak et al., 2000; Aleksandrzak-Piekarczyk et al., 2005). The CcpA protein is a member of the LacI-GalR family of bacterial repressors and exists only in Gram-positive bacteria (Weickert & Adhya, 1992). It exerts its regulatory role in carbon catabolite repression (CCR) by binding to DNA sites called cres, which occur in the vicinity of CcpA-regulated genes (Weickert & Chambliss, 1990). In L. lactis the known targets of CcpA are the gal operon for galactose utilization (Luesink et al., 1998), the fru operon for fructose utilization (Barrière et al., 2005), the ptcABC operon for cellobiose utilization (Zomer et al., 2007), and cel-lac genes for cellobiose and lactose utilization (Aleksandrzak-Piekarczyk et al., 2011). Thus, one could speculate that in L. lactis IL1403 cellobiose-inducible chromosomal alternative lactose utilization genes are under the negative control of CcpA, and, therefore, inactivation of the ccpA gene could result in their derepression and ability to assimilate lactose by the IL1403 ccpA mutant.
Further studies of Aleksandrzak-Piekarczyk et al. (2005, 2011) and Kowalczyk et al. (2008) provided details on interconnected metabolism of β-glucosides (cellobiose) and β-galactosides (lactose) and its variable regulation in L. lactis IL1403. Several genes have been implicated in coupled cellobiose and lactose assimilation in L. lactis IL1403, such as bglS and celB, ptcA and ptcB, encoding proteins homologous to P-β-glucosidase and EII components of cellobiose-specific PTS, respectively (Fig. 1). It has been shown that in L. lactis IL1403 the cellobiose-specific PTS system, comprising of celB, ptcB and ptcA, is also able to transport lactose because cellobiose-specific permease CelB has also an affinity for lactose, and, moreover, is the only permease involved in lactose uptake (Aleksandrzak-Piekarczyk et al., 2011). Furthermore, internalized lactose-P is hydrolyzed exclusively by BglS – an enzyme with dual P-β-glucosidase and P-β-galactosidase activity, and high affinity for cellobiose (Aleksandrzak-Piekarczyk et al., 2005) (Fig. 1). Thus, BglS activity generates glucose and galactose-P molecules. Glucose enters the Embden-Meyerhof-Parnas glycolytic pathway through phosphorylation by glucokinase, whereas galactose-P requires dephosphorylation performed by an unidentified phosphatase or phosphohexomutase, before entering the Leloir pathway (Neves et al., 2010) (Fig. 1). Moreover, this alternative lactose utilization system has been shown to be tightly controlled by CcpA-directed negative regulation (Fig. 1), since inactivation of the ccpA gene led to derepression of bglS, celB, ptcA and ptcB and L. lactis IL1403 ccpA mutant ability to assimilate lactose (Aleksandrzak-Piekarczyk et al., 2011). In addition to CcpA-mediated repression, the celB and bglS genes are specifically activated by cellobiose, as its presence leads to an increase in their transcription. This phenomenon has not been observed when other sugars, such as glucose, galactose or salicin, were used as carbon sources (Aleksandrzak-Piekarczyk et al., 2011). Preliminary results suggest that a hypothetical transcriptional regulator, namely YebF, could be engaged in this cellobiose-dependent activation of celB and bglS (Aleksandrzak-Piekarczyk et al., 2011; unpublished personal analysis) (Fig. 1). The YebF protein belongs to the RpiR family of phosphosugar binding proteins (Sorensen & Hove-Jensen, 1996), and, in addition to its sugar binding domain (SIS), it has a putative helix-turn-helix (HTH) DNA-binding domain. In addition to yebF mutant ferment lactose inability (Aleksandrzak-Piekarczyk et al., 2005), inactivation of the yebF gene in IL1403 resulted in inability to grow on cellobiose (unpublished personal analysis), suggesting the gene’s requirement in both cellobiose and lactose assimilation. Further studies on this phenomenon in L. lactis are needed to address it in greater detail.
When cellobiose is available, it activates the cellobiose-specific PTS transport system, comprising CelB, PtcB and PtcA proteins, and L. lactis IL1403 is able to grow on cellobiose and lactose. This growth is supported by the activity of cellobiose-inducible BglS protein, which splits lactose-P into galactose-P and glucose. Then, after the dephosphorylation step, galactose is further metabolized through the Leloir pathway, while glucose enters glycolysis. Therefore, inactivation of the ccpA gene results in derepression of the cellobiose-specific PTS transport system and also of the bglS gene, which in turn enable the IL1403 strain to grow on lactose.
Schematic representation of the proposed mechanism of chromosomally-encoded lactose, cellobiose-inducible lactose and β-glucosides metabolism and of its regulation in L. lactis IL1403. In this model the key elements are the CelB, PtcB, PtcA, BglS and PtbA proteins. In the presence of glucose, IL1403 is unable to assimilate either lactose or β-glucosides. Under these conditions, these catabolic systems are either repressed by the CcpA protein and/or are not induced by the BglR activator.
Besides cellobiose, other β-glucosides like arbutin, esculin and salicin are transported by the PtbA-mediated PTS system. In the absence of any of these three sugars, ptbA expression is not induced by the inactive the phosphorylated BglR antiterminator protein. Once a β-glucoside is available, BglR becomes dephosphorylated and active, inducing the expression of the ptbA gene. The PtbA protein transports, with concomitant phosphorylation, arbutin, esculin and salicin, which are then probably hydrolyzed by BglH, a P-β-glucosidase, encoded by a gene located downstream of and in the same operon as the ptbA gene.
It is also proposed in this model that LacS is not engaged in lactose internalization and its function is limited to galactose transport.
Despite the fact that the metabolism of lactose and β-glucosides is very important for the biotechnological processes catalysed by L. lactis, thorough studies of the chromosomally encoded features enabling use of these carbon sources were so far rather scarce. The reason for this could be the fact that L. lactis demonstrates a very large and complex metabolic capability towards carbohydrates used as carbon and energy sources, and, moreover, that this genetic potential is tightly regulated by various environmental and intracellular factors. It seems that the main obstacle in studies on the complicated mechanisms involved in assimilation of β–glycoside sugars was the lack of complex data specifying the sequences of genes potentially involved in the metabolism of these sugars and its regulation. Indeed, recent access to the genomic sequences of some these bacteria greatly advanced the research on the metabolism of various β–glycosides. As expected, the results of sequencing of lactococcal genomes and genes annotations confirmed that there are numerous genes encoding potential β-glucosides-specific transport systems and β-glucosidases, sometimes with dual activities. And, to complicate the matter even further, the analysis of the list of genes annotated in L. lactis leads to over a hundred transcriptional regulators. A relatively large number of them may be related to carbon metabolism control. These regulators, together with signals modulating their activity, and the controlled genes form a regulatory network that is necessary for sensing the environmental conditions and adjusting the catabolic capacities of the cell.
Detailed knowledge of sugar metabolism and the regulators controlling gene expression in Lactococcus lactis may contribute to the improvement of mechanisms controlling significant cellular processes in these bacteria. In the case of industrial microorganisms, acting on the defined regulatory network may drastically affect the properties of the bacteria and have an impact on bioprocesses.
Lastly, is shown as an example that by the use of a simple microbiological screen, it is possible and worthwhile to modify the metabolic potential of lactococcal strains initially unable to assimilate lactose. By inactivation of the ccpA gene or induction of particular genes by supplementation of the medium with cellobiose and thus activation of YebF, it is possible to turn on an alternative lactose assimilation pathway in L. lactis IL1403. In contrast to plasmid-located lac-operons, the cel-lac system is within the chromosome, resulting in a stable, highly adapted strain, potentially valuable for the dairy industry.
Some of the data presented were funded in part by the NCN grant UMO-2011/01/B/ NZ2/05377.
Pump intake is the part of a pump that draws fluid from the reservoir called the sump as a result of pressure difference generated by the impeller. In most cases, pumped fluid enters the intake in a swirling motion due to geometric features of the sump [1]. Inappropriate sump design such as abrupt changes in sump boundaries, narrow clearance under the pump inlet and asymmetric orientation of the approach channel to the sump will lead to the formation of swirls and vortices [2]. Strong vortices may cause damages to the pump impeller by channelling air to the impeller surface and initiate adverse effects such as cavitation and vibration [3]. On the other hand, excessive swirls in the intake flow can impose imbalance loading to the impeller and even bring resistance to the impeller rotation by introducing swirl rotation in the opposite direction [4]. Due to site condition and operational restrictions, optimal sump design may not be achieved, and therefore local flow correction devices are used as remedial measures.
\nThese devices which are commonly known as anti-vortex device (AVD) come in different shapes and sizes, depending on its application. The conceptual design of AVD is outlined in ANSI/HI 9.8-2018 [5] standard which is a guideline to assist engineers and designers in optimal intake sump design. Among the AVD types employed in real applications are floor splitter [6], floor cone [7] and corner fillet [8]. These AVD types serve the purpose of eliminating submerged vortices formed at the sump floor. Floor splitters are the most widely used AVD type due to its effectiveness in eliminating vortices and reducing vorticity in the pump intake flow. There are two versions of floor splitter, namely the prism and the plate types. The use of plate type floor splitter is favourable in many applications due to its fabrication friendly-feature and economic design [9]. However, there are a limited number of articles in the literature which discuss the features of floor splitter plate in detail. In this chapter, the characteristics of swirl angle reduction of a floor splitter plate installed in pump sump are studied.
\nThe study was carried out by both experimental and numerical approaches. A single intake pump sump model, as shown in \nFigure 1\n, was utilized for the study in which the sample of a floor splitter was installed beneath an intake suction pipe in the sump model. The layout of the sump model test section and the dimensions of the floor splitter installed is illustrated in \nFigure 2(a)\n and \n(b)\n, respectively.
\nThe experimental rig.
Main dimensions of the sump model and splitter.
The main objective of the study is to evaluate the swirling motion in the intake pipe and associated with submerged vortex without and with the installation of floor splitter plate. Initially, the experiment was conducted without the installation of floor splitter plate to capture the initial conditions of the setup. The measurement of the intensity of swirl in the intake pipe was performed according to the procedure described in ANSI/HI 9.8-2018 standard for pump sump model test. The parameter used to quantify the measurement data is the swirl angle θ which is defined in the following equation:
\nwhere d is the inner diameter of the intake pipe, n is the revolution count of the measurement instrument called the swirl metre and a is the average axial velocity at the location of the swirl metre. The swirl metre consists of a shaft with four straight blades used to capture the swirling motion in the intake pipe, and the revolution count of the swirl metre blade is measured using a tachometer. \nFigure 3\n shows typical swirl metre installation according to ANSI/HI 9.8-2018 standard. Basically, θ is the convention for describing the ratio between the axial velocity and the tangential velocity of the intake flow which characterizes the intensity of the swirling motion in the fluid. The acceptance criteria according to ANSI/HI 9.8-2018 is that the swirl angle must be lower than 5° to prevent excessive swirl in the intake flow.
\nSwirl metre installation according to ANSI/HI 9.8-2018 standard.
In order to generate the submerged vortex, the clearance under the pipe was set to 0.3 times the diameter of the inlet D and two types of flow conditioners were installed: a sloped floor with an inclination angle of 30° and a sloped wall with the same inclination angle. These flow conditioners were installed at a distance of about 5D from the centre of the intake pipe as shown in \nFigure 4(a)\n and \n(b)\n, respectively. The measurement was conducted in a range of pump submergence levels which are normalized by the minimum inlet submergence Smin\n, a threshold value before the occurrence of a surface vortex. Smin\n is calculated by the following equation:
\nFalse floor and false wall arrangements.
\nFrin\n is the Froude number at the pipe inlet and is given by:
\nwhere νin\n is the flow velocity at the inlet and g is the gravitational acceleration. The range of the dimensionless parameter S/Smin\n was set between 0.8 and 1.2.
\nThe numerical approach part of the study is set for the simulation of the flow in a full-scale pump sump. As the construction cost for a full-scale pump sump cannot be afforded, a computational fluid dynamics (CFD) simulation was employed as a replacement. The numerical model was validated with experimental data and incorporated with a combined flow conditioner that consists of inclined floor and inclined wall as the ones used in the experiment and built at a scale of 9:1. The flow rate of the pump was set to 2170 l/s, and the pump submergence took the value of Smin\n which is, after the calculation by using Eq. (2), equals to 2678 mm. The mesh structure and the dimensions of the full-scale pump sump are illustrated in \nFigures 5\n and \n6\n, respectively, while the values of the model dimensions are listed in \nTable 1\n.
\nNumerical model of the full-scale pump sump; (a) the computational domain, (b) model without floor splitter plate, (c) model with floor splitter plate.
Dimensions of the full-scale model.
Parameter | \nDimension (mm) | \n
---|---|
Inlet diameter D\n | \n1275 | \n
Pipe diameter d\n | \n850 | \n
Right side distance W1 | \n1190 | \n
Left side distance W2 | \n1360 | \n
Water entrance width W3 | \n1275 | \n
Intake pipe height H1 | \n9350 | \n
Sump height H2 | \n4250 | \n
Water entrance height H3 | \n2975 | \n
Floor length L1 | \n6375 | \n
Water entrance distance from sloped floor L2 | \n8417 | \n
Clearance C\n | \n382.5 | \n
Dimension values of the full-scale model shown in \nFigure 6\n.
\n\nFigures 7\n and \n8\n show the distribution of swirl angle values at different submergence ratios in the case of false floor and false wall flow conditioner, respectively. Generally, the installation of floor splitter plate has shown reduction in the swirl angle values. The parameter that can be used to characterize the reduction effect of the floor splitter plate is the swirl angle reduction factor Rθ\n which is defined as follows:
\nSwirl angle values at different submergence ratios for the false floor case.
Swirl angle values at different submergence ratios for the false wall case.
In this experiment, the average value of Rθ\n for the false floor case is 1.53, while in the false wall case, the average value of Rθ\n is 1.62. In \nFigure 7\n, the swirl angle values show a decreasing trend with increasing submergence ratio for S/Smin\n greater than 1 when installed with floor splitter plate. This is due to the fact that for S/Smin\n greater than 1, there was only a submerged vortex present in the sump. As the function of floor splitter plate is to eliminate submerged vortices, this result proved that the installation of floor splitter plate has served the purpose. When S/Smin\n is decreased below 1, the swirl angle values increase with decreasing submergence ratio. The inception of free surface vortex at S/Smin\n below 1 has caused bigger fluctuation in swirl angle as can be seen in the larger uncertainties within this region. The higher swirl angle values are contributed by the increase in approach flow velocity at lower water levels. The floor splitter vortex has shown limited swirl angle reduction effect if the submergence ratio is decreased below 1.
\nIn \nFigure 8\n, the swirl angle values show a sinusoidal trend with increasing submergence ratio for S/Smin\n greater than 1 when installed with floor splitter plate. The trend is contributed by the inception of free surface vortex at S/Smin\n greater than 1. Although the theory behind the minimum inlet submergence Smin\n is that there should be no free surface vortex formed in the sump if the submergence S is greater than Smin\n, this deviation from the theory was contributed by the use of false wall in which the flow has been prerotated at the beginning of the sump. The prerotation has therefore caused the flow to develop a free surface vortex earlier than expected. In the experiment, this situation occurred at S/Smin\n = 1.15. As the swirl angle decreases when S/Smin\n decreases below 1.15, the reduction effect of the floor splitter plate can be observed in the decreasing trend of the swirl angle values. Similar to the case of false floor, the swirl angle increases as the submergence ratio decreases due to the increasing approach flow velocity at low water levels.
\nDespite the swirl angle reduction effect of floor splitter plate, the fulfilment of the requirement of swirl angle reduction below 5° has not been achieved for most of the cases. In the case of false floor, there is no submergence ratio value at which the swirl angle has been reduced below 5°; however, for the false wall case, the reduction of swirl angle values below 5° can be seen between S/Smin\n = 1.00 and S/Smin\n = 1.05, i.e. the requirement for all submergence ratios when installed with floor splitter plate. This result shows that there is a limiting factor that prevented the swirl angle reduction below 5° and that factor lies on the design of the floor splitter as suggested by Kang et al. [9].
\nThe first part of the discussion on the result of simulation of flow in full-scale pump sump model is about the vortex elimination by the installation of floor splitter plate. The evaluation is based on the vorticity in the y-axis ωy\n due to its influence on the swirling motion of the flow. The value of ωy\n is normalized by the ratio of velocity in the suction pipe and the pipe inner diameter νd/d. \nFigure 9\n shows the cross section along x-y plane in which the evaluation of the result in the streamwise direction takes place and its corresponding results which are shown in \nFigure 10\n.
\nEvaluation area in x-y plane of the pump sump model (z = 1600 mm).
Contour plot of ωy/(νd/d) at the location of vortex in x-y plane; (a) without floor splitter plate, (b) with floor splitter plate. Dashed circular lines denote pipe diameter.
From \nFigure 10\n, it can be observed that the core of the vortex, indicated by the high-intensity region extending from the floor towards inside of the pump, has been eliminated with the installation of floor splitter plate. The vorticity in the pipe has also been reduced which can be seen from the contour colors. The velocity vectors, which appear to point diagonally to the left indicating a strong swirling flow in the pipe, have been straightened in a direction vertically upward towards the direction of suction when installed with floor splitter plate.
\nWhen observing the cross section in the spanwise direction (in the plane illustrated in \nFigure 11\n), similar results are presented. Basically the flow that enters the pump is divided into two regions, namely the right side and the left side flow, due to the geometry of the sump. The flow entrance velocity from the right and the left side of the inlet are nearly the same because of the nearly symmetrical positioning of the pump. The flow entered the pump in a spiral manner without the installation of floor splitter which resulted in vortex formation near to the left side of the pump. When installed with floor splitter plate, the flow is reorganized, and therefore the spiral motion of the flow has been reduced and hence the vortex eliminated. This situation is reflected by the discontinued vortex core shown in \nFigure 12\n with the installation of floor splitter plate.
\nEvaluation area in y-z plane of the pump sump model (x = 15,860 mm).
Contour plot of ωy/(νd/d) at the location of vortex in y-z plane; (a) without floor splitter plate, (b) with floor splitter plate.
As the main function of floor splitter plate is to eliminate vortices formed at the sump floor, an evaluation about the vorticity in the plane at the sump floor is necessary. This location is shown in \nFigure 13\n. The vortex core is indicated by the spiralling streamline under the pump inlet which can be seen in \nFigure 14\n in the case without floor splitter plate. As the floor splitter plate was installed, the path of the spiral streamline was interrupted by the plate, and therefore the formation of vortex was prevented. Due to the suction by the pump, a small vortex attached to the side of the floor splitter plate was formed which is inherited from the flow without floor splitter plate as shown in \nFigure 14(b)\n. However, this vortex constitutes a much smaller vortex core diameter (estimated to be less than 0.1D based on the scale at the x-axis of the graph) and relatively weak compared to the large vortex (estimated to be about 0.2D) which can be seen in \nFigure 14(a)\n, and therefore it can be considered as nondestructive to the pump impeller.
\nEvaluation area in z-x plane of the pump sump model (y = 10 mm).
Contour plot of ωy/(νd/d) at the floor of the sump in z-x plane; (a) without floor splitter plate, (b) with floor splitter plate.
The next part of the evaluation is about the swirl angle reduction characteristics of floor splitter plate installation. For this purpose, an evaluation plane was selected at the position comparable to the installation of swirl metre in the experimental model. The location of the plane is shown in \nFigure 15\n, and its corresponding results are displayed in in \nFigure 16\n. The flow at the swirl metre location was rotational with relatively high velocity components as indicated by the velocity vectors. The two visible vorticity regions show the divided inflow field in the pipe as explained in the previous paragraph which is considerably high in reference to the value of νd/d as shown in \nFigure 16\n. With the installation of floor splitter, the magnitude of both vorticity regions is significantly reduced and the resulting velocity vectors are also smaller in size compared to the case without floor splitter. This indicates that the spiral flow has been dissolved by the floor splitter plate into a relatively straight flow and the outcome is consistent with the experimental result presented in the previous subsection.
\nEvaluation area at the position of swirl metre in z-x plane of the pump sump model (y = 4250 mm).
Contour plot of ωy/(νd/d) at the swirl metre position in z-x plane; (a) without floor splitter plate, (b) with floor splitter plate.
To get a better understanding about the result, a 3D streamline visualization of the intake flow in the sump is illustrated for every case as comparison in \nFigure 18\n. It can be seen that the intake flow was spiral before the installation of floor splitter plate and as the floor splitter was installed, the spiral motion of the flow was dissolved and went into a relatively straight path. Quantitative values can also be extracted from the result to obtain the associated swirl angle values. The approach for the calculation of swirl angle from the simulation results is based on the principle of Eq. (1) itself where by definition the swirl angle is the angle between the velocity components of the intake flow in the axial and tangential direction. From Eq. (1), the term πdn represents the tangential velocity component, while the term v represents the axial velocity component; both are at the location of the swirl metre used in the experiment. \nFigure 17\n shows the velocity triangle diagram which shows the relationship between swirl angle and both of the velocity components in a schematic representation.
\nSwirl angle definition using velocity triangle diagram as shown in Kang et al. [9].
3D streamline plot showing the intake flow in the sump with the seeding of the flow starts at the floor of the sump; (a) without floor splitter plate, (b) with floor splitter plate.
Based on this approach in Eq. (1), the velocity components in the axial and tangential direction were derived from the simulation results. As the result was given in vorticity values, the tangential velocity component must be derived from the angular velocity which equals to half of the vorticity [10]. The vorticity of the flow at the position of the swirl metre is calculated by the integration of the vorticity in the plane and divided by the cross section to obtain the vorticity value per unit area. After getting the value of angular velocity, the following correlation is used to calculate the tangential velocity:
\nThe method to derive the value of axial velocity component from the results was based on the same principle in which the integral value of axial velocity component in the plane was extracted and divided by cross-sectional area of the pipe at the swirl metre location to get the velocity per unit area. The reason of performing integration to find the velocity values is that the swirling motion of the intake flow in the pipe constitutes a solid body rotation and the swirl angle value describes the rotation body as a whole [1], and this is where the integration of the velocity across the cross-sectional area becomes the most practical way of calculating the swirl angle in the simulation. After obtaining both velocity values, the swirl angle was then calculated using the velocity triangle diagram as shown in \nFigure 17\n.
\nBy following the described procedure, the swirl angle value for the case without floor splitter plate installation is 7.58°, while for the case with floor splitter plate, the swirl angle value is 4.09°. Although these values are based on average velocities as the simulation was conducted in a steady-state simulation and therefore are much smaller than the actual swirl angle values, it can be considered as adequate because they are used for comparison purpose and not for the determination of absolute values. Once again, the results are in agreement with the experimental data. This study complements a previous experimental investigation in which the effects of floor splitter heights have been analysed [11].
\nA study on the application of vortex control principle at pump intake was carried out by using an anti-vortex device type called the floor splitter plate. The device was installed in a pump sump model to eliminate vortices formed at the intake and reduce the swirling motion in the intake pipe as a method to improve pump efficiency in actual applications. Evaluation of the effect was conducted based on experimental and numerical approaches. The experimental part comprised swirl angle measurement which was performed according to ANSI/HI 9.8-2018 standard. To complement the results obtained in the experiment, a numerical simulation of the flow in a full-scale pump sump was conducted. The results showed that the installation of floor splitter plate has successfully eliminated the vortex formed at the sump floor and reduced the swirl angle in the intake flow. However, the reduction effect was not sufficient to achieve the criteria set in the ANSI/HI 9.8-2018 standard which requires the swirl angle to be less than 5°, and therefore optimization of the floor splitter plate design is needed. The simulation of flow in a full-scale pump sump produced similar findings with the experimental results. From the contour and streamline plot, it was found that the immersion of the floor splitter plate has disrupted the vortical flow under the pump inlet and provided a flow straightening effect to eliminate destructive vortices and reduce swirl angle in the pump intake.
\nThe research has been funded by the Ministry of Energy, Science, Technology, Environment and Climate Change (MESTECC), Malaysia, under Science Fund grant No. SF1326 and carried out in collaboration with the Department of Irrigation and Drainage (DID), Malaysia.
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