Relevant bibliographies by topics / Enzymes – Industrial applications

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Enzymes – Industrial applications'

Author: Grafiati
Published: 4 June 2021
Last updated: 29 January 2023

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Journal articles on the topic "Enzymes – Industrial applications"

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Ghaffari-Moghaddam, M., H. Eslahi, D. Omay, and E. Zakipour-Rahimabadi. "Industrial applications of enzymes." Review Journal of Chemistry 4, no. 4 (2014): 341–61. http://dx.doi.org/10.1134/s2079978014040037.

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Robic, Audrey, Christophe Ullmann, Pascal Auffray, Cécile Persillon, and Juliette Martin. "Enzymes for industrial applications." OCL 24, no. 4 (2017): D404. http://dx.doi.org/10.1051/ocl/2017027.

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Demain, Arnold L., and Sergio Sánchez. "Enzymes of industrial interest." Mexican journal of biotechnology 2, no. 2 (2017): 74–97. http://dx.doi.org/10.29267/mxjb.2017.2.2.74.

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For many years, industrial enzymes have played an important role in the benefit of our society due to their many useful properties and a wide range of applications. They are key elements in the progress of many industries including foods, beverages, pharmaceuticals, diagnostics, therapy, personal care, animal feed, detergents, pulp and paper, textiles, leather, chemicals and biofuels. During recent decades, microbial enzymes have replaced many plant and animal enzymes. This is because microbial enzymes are widely available and produced economically in short fermentations and inexpensive media. Screening is simple, and strain improvement for increased production has been very successful. The advances in recombinant DNA technology have had a major effect on production levels of enzymes and represent a way to overproduce industrially important microbial, plant and animal enzymes. It has been calculated that 50-60% of the world enzyme market is supplied with recombinant enzymes. Molecular methods, including genomics and metagenomics, are being used for the discovery of new enzymes from microbes. Also, directed evolution has allowed the design of enzyme specificities and better performance.
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Zamost, Bruce L., Henrik K. Nielsen, and Robert L. Starnes. "Thermostable enzymes for industrial applications." Journal of Industrial Microbiology 8, no. 2 (1991): 71–81. http://dx.doi.org/10.1007/bf01578757.

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Singh, Rajesh Kumar, Pratiksha Singh, Mohini Prabha Singh та ін. "Yeast α-L-Rhamnosidase: Sources, Properties, and Industrial Applications". SDRP Journal of Food Science & Technology 6, № 1 (2021): 313–24. http://dx.doi.org/10.25177/jfst.6.1.ra.10742.

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Yeasts have been used for the heterologous production of a range of enzymes. However, α-L-rhamnosidase production in yeasts as well as its vast potential for biotechnological processes is less reported. α-L-Rhamnosidase is one of the important biotechnologically attractive enzymes in several industrial and biotechnological processes. In food and agriculture industries, the enzyme catalyzes the hydrolysis of hesperidin to release L-rhamnose and hesperidin glucoside, industrial removal of bitterness from citrus juices caused by naringin, and enhancing aroma in grape juices and derived beverages. In pharmaceutical and chemical industries, this enzyme is used in the structural determination of polysaccharides, glycosides and glycolipids, metabolism of gellan, conversion of chloropolysporin B to chloropolysporin C, and production of prunin. Rhamnosidases are extensively distributed in fungi and bacteria while their production from yeast sources is less reported. Yeast rhamnosidase is very important as it is produced in short-duration fermentation, with enhanced shelf life, high thermal stability, capable of retaining juice flavor, and is non-toxic for human consumption. In this review, an attempt has been made to fill up this gap by focusing on production, purification, characterization, structural and molecular biological studies of yeast rhamnosidase and its potential biotechnological applications. Keywords: Industrial applications, Naringin, Rhamnosidase, Yeast
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Joshi, Ritika, and Arindam Kuila. "Lipase and their different industrial applications: A review." Brazilian Journal of Biological Sciences 5, no. 10 (2018): 237–47. http://dx.doi.org/10.21472/bjbs.051004.

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Enzymes are also known natural catalysts. Lipases are flexible enzymes that are mostly used. These enzymes are found extensively all over the animal and plant kingdoms, likewise in molds and bacteria. Among all identified enzymes, lipases have concerned the mainly biotechnological attention. This review paper discusses the characteristic, microbial origin and application of lipases. The present review discussed about different characteristics and sources (fungal, bacteria’s) of lipase. The present article also discussed about different bioreactors used for lipase production and different biotechnological applications (food, detergent, paper and pulp, biofuels etc) of lipases. An observation to considerate lipases and their applications as bulk enzymes and high-value of production, these enzymes are having huge impact in different bioprocesses.
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Littlechild, Jennifer A. "Archaeal Enzymes and Applications in Industrial Biocatalysts." Archaea 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/147671.

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Archaeal enzymes are playing an important role in industrial biotechnology. Many representatives of organisms living in “extreme” conditions, the so-called Extremophiles, belong to the archaeal kingdom of life. This paper will review studies carried by the Exeter group and others regarding archaeal enzymes that have important applications in commercial biocatalysis. Some of these biocatalysts are already being used in large scale industrial processes for the production of optically pure drug intermediates and amino acids and their analogues. Other enzymes have been characterised at laboratory scale regarding their substrate specificity and properties for potential industrial application. The increasing availability of DNA sequences from new archaeal species and metagenomes will provide a continuing resource to identify new enzymes of commercial interest using both bioinformatics and screening approaches.
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Kleiner, Leslie. "Industrial applications of enzymes in Latin America." INFORM International News on Fats, Oils, and Related Materials 28, no. 8 (2017): 38–39. http://dx.doi.org/10.21748/inform.09.2017.38.

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de Miguel Bouzas, Trinidad, Jorge Barros-Velazquez, and Tomas Gonzalez Villa. "Industrial Applications of Hyperthermophilic Enzymes: A Review." Protein & Peptide Letters 13, no. 7 (2006): 645–51. http://dx.doi.org/10.2174/092986606777790548.

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Wackett, Lawrence P. "Industrial applications of microbial salt-tolerant enzymes." Microbial Biotechnology 5, no. 5 (2012): 668–69. http://dx.doi.org/10.1111/j.1751-7915.2012.00355.x.

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Dissertations / Theses on the topic "Enzymes – Industrial applications"

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Thuku, Robert Ndoria. "The structure of the nitrilase from Rhodococcus Rhodochrous J1: homology modeling and three-dimensional reconstruction." Thesis, University of the Western Cape, 2006. http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_3225_1188474860.

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<p>The nitrilases are an important class of industrial enzymes that are found in all phyla. These enzymes are expressed widely in prokaryotes and eukaryotes. Nitrilases convert nitriles to corresponding acids and ammonia. They are used in industry as biocatalysts because of their specificity and enantioselectivity. These enzymes belong to the nitrilase superfamily in which members share a common &alpha<br>&beta<br>&beta<br>&alpha<br>structural fold and a unique cys, glu,lys catalytic triad with divergent N- and C-terminals.</p> <p>There are four atomic structures of distant homologues in the superfamily, namely 1ems, 1erz, 1f89 and 1j31. All structures have two-fold symmetry which conserves the &alpha<br>&beta<br>&beta<br>&alpha<br>-&alpha<br>&beta<br>&beta<br>&alpha<br>fold across the dimer interface known as the A surface. The construction of a 3D model based on the solved structures revealed the enzyme has two significant insertions in its sequence relative to the solved structures, which possibly correspond to the C surface. In addition there are intermolecular interactions in a region of a conserved helix, called the D surface. These surfaces contribute additional interactions responsible for spiral formation and are absent in the atomic resolution homologues.</p> <p>The recombinant enzyme from R.rhodochrous J1 was expressed in E. coli BL21 cells and eluted by gel filtration chromatography as an active 480 kDa oligomer and an inactive 80 kDa dimer in the absence of benzonitrile. This contradicts previous observations, which reported the native enzyme exists as an inactive dimer and elutes as a decamer in the presence benzonitrile. Reducing SDS-PAGE showed a subunit atomic mass of ~40 kDa. EM and image analysis revealed single particles of various shapes and sizes, including c-shaped particles, which could not form spirals due to steric hindrances in its C terminal.</p> <p>Chromatographic re-elution of an active fraction of 1-month old J1 nitrilase enabled us to identify an active form with a mass greater than 1.5 MDa. Reducing SDS-PAGE, N-terminal sequencing and mass spectroscopy showed the molecular weight was ~36.5 kDa as result of specific proteolysis in its C terminal. EM revealed the enzyme forms regular long fibres. Micrographs (109) were recorded on film using a JEOL 1200EXII operating at 120 kV at 50K magnification. Two independent 3D reconstructions were generated using the IHRSR algorithm executed in SPIDER. These converged to the same structure and the resolution using the FSC 0.5 criterion was 1.7 nm.</p> <p>The helix structure has a diameter of 13nm with ~5 dimers per turn in a pitch of 77.23 &Aring<br>. Homology modeling and subsequent fitting into the EM map has revealed the helix is built primarily from dimers, which interact via the C and D surfaces. The residues, which potentially interact across the D surface, have been identified and these confer stability to the helix. The conservation of the insertions and the possibility of salt bridge formation on the D surface suggest that spiral formation is common among microbial nitrilases. Furthermore, the presence of the C terminal domain in J1 nitrilase creates a steric hindrance that prevents spiral formation. When this is lost &ndash<br>either by specific proteolysis or autolysis - an active helix is formed.</p>
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De, Rose Simone Antonio. "Stabilisation of lipolytic enzymes for industrial applications." Thesis, University of Exeter, 2017. http://hdl.handle.net/10871/32824.

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The use of enzymes as industrial catalysts is a very promising alternative to conventional synthetic chemistry since enzymes are very specific, selective and display very high activity under mild experimental conditions. This research is focused on lipases, which are widely used in several industrial sectors and especially in the laundry industry. Enzymes in laundry formulation are exposed to alkaline pH, high concentrations of detergents and the presence of proteases. These harsh conditions have a negative effect on the stability and activity of the enzymes and can eliminate the benefits of adding enzymes to formulation entirely. This study aimed to investigate the stabilisation of existing commercial lipases and the characterisation of a novel cold-adapted lipase for industrial applications. The commercial lipase Lipex 16L is a variant of the Thermomyces lanuginosus lipase and is the current benchmark lipase for application in laundry products. Lipex 16L has been used to develop an improved method for carrier-free immobilisation, using Cross-Linked Enzyme Aggregates (CLEAs). The CLEAs production protocol has been modified by introduction of an activator step to obtain a higher number of individual lipase molecules in the "open lid" conformation and by the introduction of a terminator step to quench the cross-linking reaction at an optimal time to obtain smaller and more homogenous cross-linked particles. This improved immobilisation method has been compared to a commercially available immobilised enzyme and has been shown to be made up of smaller and more homogenous particles with higher activity than the Lipex 16L. The CLEAs produced show improved features for commercial applications such as an enhanced wash performance comparable with the free enzyme, improved stability to proteolysis and a higher activity after long-term storage. The stabilisation of Lipex 16L has also been investigated through the introduction of two additional glycosylation sites on the protein surface. The commercial Lipex 16L has only one glycosylation site on asparagine 33. A tri-glycosylated mutant has been generated with the introduction of two further glycosylation sites on asparagine 37 and asparagine 99. This recombinant enzyme and a mono-glycosylated wild-type enzyme have been cloned and expressed in Pichia pastoris while a non-glycosylated variant has been expressed in Escherichia coli. The enzymatic activities of the glycosylated and non-glycosylated lipases have been compared under various conditions such as temperature, pH, detergents, and incubation with proteases. The results have demonstrated that while the additional glycans do not affect the lipase activity and cleaning performance, they do improve its resistance to proteases and its overall stability with an increase of the melting temperature of + 4 °C. A novel lipase from the psychrophilic bacteria Psychromonas ingrahamii (PinLip) has been biochemically characterised. The enzyme shows activity towards short and medium chain fatty acids and has a good fat stain cleaning performance which makes it attractive for industrial applications. Structural characterisation of the PinLip has been attempted by using crystallisation trials for X-ray crystallography and NMR spectroscopy with limited success. A 3D homology model has been generated using the server I-TASSER using the most closely related known structures, Gibberella zeae, Rhizomucor miehei and Rhizopus microspores lipases, all with a sequence identity to PinLip between 20 and 24%. The different lipases studied in this thesis have been tested for their stability in the presence of traditional laundry formulation ingredients and new novel biosurfactants using differential scanning fluorimetry (DSF). The results have shown an improved stability of all the Lipex variants in presence of mono-rhamnolipids based biosurfactant, while the cold-adapted PinLip was stabilised by a small concentration of a polymer (EPEI) and few other compounds (Tinopal CBS-CL, and Triethylamine). The improved CLEAs method and the use of the PinLip enzyme have been patented (Patent no: WO2017/036901, WO2017/036902, WO2017/036915, WO2017/036916, and WO2017/036917).
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Tsekoa, Tsepo L. "Structure, enzymology and genetic engineering of Bacillus sp. RAPc8 nitrile hydratase." Thesis, University of the Western Cape, 2005. http://etd.uwc.ac.za/index.php?module=etd&amp.

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Microbial nitrile hydratases are important industrial enzymes that catalyse the conversion of nitriles to the corresponding amides. A thermostable, cobalt-type Bacillus sp. RAPc8 microbial nitrile hydratase was cloned and expressed in E.coli. In this study the primary aim was to determine the molecular structure of Bacillus sp. RAPc8 microbial nitrile hydratase.
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De, Villiers Tania. "Fungal enzymes and microbial systems for industrial processing." Thesis, Stellenbosch : Stellenbosch University, 2008. http://hdl.handle.net/10019.1/21457.

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Thesis (PhD)--Stellenbosch University, 2008.<br>ENGLISH ABSTRACT: This study strives to improve two current industrial processes by making them more cost effective through the use of hydrolytic enzymes or microbial systems. The first process targeted is the industrial conversion of starch to ethanol. In the second process, hydrolytic enzymes are applied to the manufacturing of instant coffee. The engineering of microbial systems to convert starch to bio-ethanol in a one-step process may result in large cost reductions in current industrial processes. These reductions will be due to decreased heating energy requirements, as well as a decrease in money spent on the purchase of commercial enzymes for liquefaction and saccharification. In this study, a recombinant Saccharomyces cerevisiae strain was engineered to express the wild-type Aspergillus awamori glucoamylase (GA I) and α-amylase (AMYL III) as well as the Aspergillus oryzae glucoamylase (GLAA) as separately secreted polypeptides. The recombinant strain that secreted functional GA I and AMYL III was able to utilise raw corn starch as carbon source, and converted raw corn starch into bio-ethanol at a specific production rate of 0.037 grams per gram dry weight cells per hour. The ethanol yield of 0.40 gram ethanol per gram available sugar from starch translated to 71% of the theoretical maximum from starch as substrate. A promising raw starch converter was therefore generated. In the second part of this study, soluble solid yields were increased by hydrolysing spent coffee ground, which is the waste generated by the existing coffee process, with hydrolytic enzymes. Recombinant enzymes secreted from engineered Aspergillus strains (β-mannanase, β-endoglucanase 1, β-endo-glucanase 2, and β-xylanase 2), enzymes secreted from wild-type organisms (β-mannanases) and commercial enzyme cocktails displaying the necessary activities (β-mannanase, cellulase, and pectinase) were applied to coffee spent ground to hydrolyse the residual 42% mannan and 51% cellulose in the substrate. Hydrolysis experiments indicated that an enzyme cocktail containing mainly β-mannanase increased soluble solids extracted substantially, and a soluble solid yield of 23% was determined using the optimised enzyme extraction process. Soluble solid yield increases during the manufacturing of instant coffee will result in; (i) an increase in overall yield of instant coffee product, (ii) a decrease in amount of coffee beans important for the production of the product, and (iii) a reduction in the amount of waste product generated by the process.<br>AFRIKAANSE OPSOMMING: Hierdie studie poog om twee huidige industriële prosesse te verbeter deur die prosesse meer kosteeffektief met behulp van hidroltiese ensieme en mikrobiese sisteme te maak. Die eerste industrie wat geteiken word, is die omskakeling van rou stysel na etanol, en die tweede om hidrolities ensieme in die vervaardiging van kitskoffie te gebruik. Die skep van mikrobiese sisteme om rou-stysel in ’n ’een-stap’ proses om te skakel na bio-etanol sal groot koste besparing tot gevolg hê. Hierdie besparings sal te wyte wees aan die afname in verhittingsenergie wat tydens die omskakelingsproses benodig word, asook ’n afname in die koste verbonde aan die aankoop van duur kommersiële ensieme om die stysel na fermenteerbare suikers af te breek. In hierdie studie is ’n rekombinante Saccharomyces cerevisiae-gis gegenereer wat die glukoamilase (GA I) and α-amilase (AMYL III) van Aspergillus awamori, asook die glukoamilase van Aspergillus oryzae (GLAA) as aparte polipeptide uit te druk. Die rekombinante gis wat die funksionele GA I en AMYL III uitgeskei het, was in staat om op die rou-stysel as koolstofbron te groei, en het roustysel na bio-etanol teen ’n spesifieke tempo van 0.037 gram per gram droë gewig biomassa per uur omgeskakel. Die etanolopbrengs van 0.40 gram per gram beskikbare suiker vanaf stysel was gelykstaande aan 71% van die teoretiese maksimum vanaf stysel as substraat. ’n Belowende gis wat roustysel kan omskakel na bio-etnaol was dus geskep. In die tweede deel van hierdie studie is die opbrengs in oplosbare vastestowwe vermeerder deur die koffie-afval wat tydens die huidige industrieële proses genereer word, met hidrolitiese ensieme te behandel. Rekombinante ensieme afkomstig vanaf Aspergillus-rasse (β-mannanase, β-endoglukanase 1, β-endo-glukanase 2 en β-xilanase 2), ensieme deur wilde-tipe organismes uitgeskei (β-mannanase), asook kommersiële ensiempreparate wat die nodige ensiemaktiwiteite getoon het (β-mannanase, sellulase en pektinase) is gebruik om die oorblywende 42% mannaan en 51% sellulose in koffie-afval te hidroliseer. Hidrolise eksperimente het getoon dat ’n ensiempreparaat wat hoofsaaklik mannanase bevat, die oplosbare vastestofopbrengs grootliks kan verbeter, met ’n verhoogde opbrengs van 23% tydens geöptimiseerde ensiembehandelings. ’n Verhoogde opbrengs in oplosbare vastestowwe tydens die vervaardiging van kitskoffie sal die volgende tot gevolg hê: (i) ’n toename in totale opbrengs van kitskoffie produk, (ii) ’n afname in die hoeveelheid koffiebone wat vir die produksie ingevoer moet word, en (iii) ’n afname in die hoeveelheid afval wat tydens die vervaardigingsproses produseer word.
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Jordaan, Justin. "Isolation and characterization of a novel thermostable and catalytically efficient laccase from Peniophora sp. strain UD4." Thesis, Rhodes University, 2005. http://eprints.ru.ac.za/211/.

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Santos, Bruna Leal dos [UNESP]. "Imobilização de lipase po diferentes técnicas para obtenção de catalizadores estáveis." Universidade Estadual Paulista (UNESP), 2014. http://hdl.handle.net/11449/108775.

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Made available in DSpace on 2014-08-13T14:50:56Z (GMT). No. of bitstreams: 0 Previous issue date: 2014-02-21Bitstream added on 2014-08-13T17:59:58Z : No. of bitstreams: 1 000768347_20160221.pdf: 161112 bytes, checksum: 81652a09b62d246f4c78fc239ef06ae2 (MD5) Bitstreams deleted on 2016-02-22T11:12:47Z: 000768347_20160221.pdf,. Added 1 bitstream(s) on 2016-02-22T11:13:41Z : No. of bitstreams: 1 000768347.pdf: 885551 bytes, checksum: 3352268d651e4caf0f5c3131e9467935 (MD5)<br>As lipases, também chamadas de glicerol éster hidrolases, são enzimas que fazem parte do grupo das serina hidrolases, tendo como substrato, triglicerídeos. O modo de ação das lipases assemelha-se ao das esterases, realizando a hidrólise das ligações ésteres-carboxílicas de acilgliceróis, formando ácidos graxos e glicerol. Processos de bioconversão enzimática têm sido bastante utilizados na produção, transformação e valorização de matérias-primas. Avanços na tecnologia enzimática, como a imobilização de enzimas, possibilitaram a modificação das propriedades cinéticas e da estabilidade destas moléculas contribuindo com o aumento no potencial de aplicações das mesmas. O presente trabalho teve por objetivo estudar diferentes métodos de imobilização de lipases em suportes de sílica, bem como os efeitos deste procedimento, visando melhorar a funcionalidade das enzimas e o maior rendimento econômico nos processos industriais. Os métodos de imobilização escolhidos para os estudos foram: adsorção física, ligação covalente e encapsulação. O processo de imobilização de lipase em Celite (adsorção física) foi otimizado levando em conta o pH, porcentagem da concentração enzima:suporte e temperatura ótimos de atividade enzimática. Também se utilizou Celite como suporte para a imobilização de lipase por ligação covalente, onde se obteve os melhores resultados com atividade enzimática 20% a 40 ºC e eficiência de imobilização de 50%. A celite foi ativada com 3-aminopropiltrietoxisilano e glutaraldeído. Por último, foi avaliada a possibilidade de encapsulação da lipase utilizando o precursor tetraetilortossilicato (TEOS). Os resultados obtidos nesta última metodologia não se mostraram satisfatórios. Logo, com os dados obtidos, podemos dizer que uma boa manutenção da atividade catalítica depende do tipo de retenção (química ou física) e da força de interação ...<br>Lipases, also known as glycerol ester hydrolases , are enzymes that belong to the group of serine hydrolases. The mode of action of lipases is very similar to esterase group, performing the hydrolysis of carboxylic esters of glycerides - forming fatty acids and glycerol. The enzymatic bioconversion processes have been widely used in manufacturing, processing and recovery of raw materials. Advances methodology for immobilization of enzyme have allowed the modification of the kinetic properties and stability of these molecules contributing to the increase in the potential applications of the same. The present work is aimed to study different methods of immobilization of lipases in silica supports, and the effects of this procedure to improve the functionality of enzymes. The immobilization methods chosen for the studies were: physical adsorption, covalent bonding and encapsulation process. The process of immobilization of lipase on Celite (by physical adsorption) was optimized taking into account several parameters such as: pH, the enzyme concentration:support and temperature for enzyme activity. Celite was also used as a support for the immobilization of lipase by covalent bond, where best results were obtained with 20% enzymatic activity at 40 ° C and immobilization efficiency of 50%. The celite was activated with 3-aminopropyltriethoxysilane and glutaraldehyde. Finally, we have studied the possibility of encapsulation of lipase using the precusor tetraethylorthosilicate (TEOS). The results of this last methodology were not satisfactory. These results show that to maintain a good catalytic activity depends on the type of immobilization chose (chemical or physical) and the strength of the interaction between the enzyme and support, which can cause structural distortions in the protein, leading maintenance or a decrease in catalytic activity
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Santos, Bruna Leal dos. "Imobilização de lipase po diferentes técnicas para obtenção de catalizadores estáveis /." Botucatu, 2014. http://hdl.handle.net/11449/108775.

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Orientador: Valter de Albuquerque Pedrosa<br>Coorientador: Luciana Francisco Fleuri<br>Banca: Maria José Queiroz de Freitas Alves<br>Banca: Haroldo Yukio Kawaguti<br>Resumo: As lipases, também chamadas de glicerol éster hidrolases, são enzimas que fazem parte do grupo das serina hidrolases, tendo como substrato, triglicerídeos. O modo de ação das lipases assemelha-se ao das esterases, realizando a hidrólise das ligações ésteres-carboxílicas de acilgliceróis, formando ácidos graxos e glicerol. Processos de bioconversão enzimática têm sido bastante utilizados na produção, transformação e valorização de matérias-primas. Avanços na tecnologia enzimática, como a imobilização de enzimas, possibilitaram a modificação das propriedades cinéticas e da estabilidade destas moléculas contribuindo com o aumento no potencial de aplicações das mesmas. O presente trabalho teve por objetivo estudar diferentes métodos de imobilização de lipases em suportes de sílica, bem como os efeitos deste procedimento, visando melhorar a funcionalidade das enzimas e o maior rendimento econômico nos processos industriais. Os métodos de imobilização escolhidos para os estudos foram: adsorção física, ligação covalente e encapsulação. O processo de imobilização de lipase em Celite (adsorção física) foi otimizado levando em conta o pH, porcentagem da concentração enzima:suporte e temperatura ótimos de atividade enzimática. Também se utilizou Celite como suporte para a imobilização de lipase por ligação covalente, onde se obteve os melhores resultados com atividade enzimática 20% a 40 ºC e eficiência de imobilização de 50%. A celite foi ativada com 3-aminopropiltrietoxisilano e glutaraldeído. Por último, foi avaliada a possibilidade de encapsulação da lipase utilizando o precursor tetraetilortossilicato (TEOS). Os resultados obtidos nesta última metodologia não se mostraram satisfatórios. Logo, com os dados obtidos, podemos dizer que uma boa manutenção da atividade catalítica depende do tipo de retenção (química ou física) e da força de interação ...<br>Abstract: Lipases, also known as glycerol ester hydrolases , are enzymes that belong to the group of serine hydrolases. The mode of action of lipases is very similar to esterase group, performing the hydrolysis of carboxylic esters of glycerides - forming fatty acids and glycerol. The enzymatic bioconversion processes have been widely used in manufacturing, processing and recovery of raw materials. Advances methodology for immobilization of enzyme have allowed the modification of the kinetic properties and stability of these molecules contributing to the increase in the potential applications of the same. The present work is aimed to study different methods of immobilization of lipases in silica supports, and the effects of this procedure to improve the functionality of enzymes. The immobilization methods chosen for the studies were: physical adsorption, covalent bonding and encapsulation process. The process of immobilization of lipase on Celite (by physical adsorption) was optimized taking into account several parameters such as: pH, the enzyme concentration:support and temperature for enzyme activity. Celite was also used as a support for the immobilization of lipase by covalent bond, where best results were obtained with 20% enzymatic activity at 40 ° C and immobilization efficiency of 50%. The celite was activated with 3-aminopropyltriethoxysilane and glutaraldehyde. Finally, we have studied the possibility of encapsulation of lipase using the precusor tetraethylorthosilicate (TEOS). The results of this last methodology were not satisfactory. These results show that to maintain a good catalytic activity depends on the type of immobilization chose (chemical or physical) and the strength of the interaction between the enzyme and support, which can cause structural distortions in the protein, leading maintenance or a decrease in catalytic activity<br>Mestre
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Musengi, Amos. "Exploitation of the potential of a novel bacterial peroxidase for the development of a new biocatalytic process." Thesis, Cape Peninsula University of Technology, 2014. http://hdl.handle.net/20.500.11838/1525.

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Thesis submitted in partial fulfilment of the requirements for the degree Doctor of Technology: Biomedical Technology In the Faculty of Health and Wellness Sciences At the Cape Peninsula University of Technology 2014<br>Peroxidases are ubiquitous catalysts that oxidise a wide variety of organic and inorganic compounds employing peroxide as the electron acceptor. They are an important class of oxidative enzymes which are found in nature, where they perform diverse physiological functions. Apart from the white rot fungi, actinomycetes are the only other known source of extracellular peroxidases. In this study, the production of extracellular peroxidase in wild type actinomycete strains was investigated, for the purpose of large-scale production and finding suitable applications. The adjustment of environmental parameters (medium components, pH, temperature and inducers) to optimise extracellular peroxidase production in five different strains was carried out. Five Streptomyces strains isolated from various natural habitats were initially selected for optimisation of their peroxidase production. Streptomyces sp. strain BSII#1 and Streptomyces sp. strain GSIII#1 exhibited the highest peroxidase activities (1.30±0.04 U ml-1 and 0.757±0.01 U ml-1, respectively) in a complex production medium at 37°C and pH 8.0 in both cases. Maximum enzyme production for Streptomyces strain BSII#1 was obtained in the presence of 0.1 mM veratryl alcohol or pyrogallol, while 0.1 mM guaiacol induced the highest peroxidase production in Streptomyces sp. strain GSIII#1. As the highest peroxidase producer, Streptomyces sp. strain BSII#1 was selected for further studies. The strain was first characterised by a polyphasic approach, and was shown to belong to the genus Streptomyces using various chemotaxonomic, genotypic and phenotypic tests. Production of peroxidase was scaled up to larger volumes in different bioreactor formats. The airlift configuration was optimal for peroxidase production, with Streptomyces sp. strain BSII#1 achieving maximum production (4.76±0.46 U ml-1) in the 3 l culture volume within 60 hrs of incubation. A protocol for the purification of the peroxidase was developed, which involved sequential steps of acid and acetone precipitation, as well as ultrafiltration. A purification factor of at least 46-fold was achieved using this method and the protein was further analysed by LC-MS. The protein was shown to be a 46 kDa protein, and further biochemical characterisation showed that the peroxidase had a narrower spectrum of substrates as compared to reports on other peroxidases derived from actinomycetes. With 2,4-dichlorophenol as the substrate, the Km and Vmax for this enzyme were 0.893 mM and 1.081 μmol min-1, respectively. The purified peroxidase was also capable of catalysing coupling reactions between several phenolic monomer pairs. Overall, the peroxidase from Streptomyces sp. strain BSII#1 could feasibly be produced in larger scales and there remains further room to investigate other potential applications for this enzyme.
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Santiago, Morcillo Gerard. "Computer-aided rational enzyme design for industrial and technological applications." Doctoral thesis, Universitat de Barcelona, 2019. http://hdl.handle.net/10803/667261.

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The massive industrial production exploited by our society since the XIX century has growth at expenses of the planet. Environmental damages are already visible, and they urge us to find new and sustainable production ways. Among all contributors, this thesis is focused on enzymes and its potential application in industry. Enzymes are biomolecules capable of performing and speeding up chemical reactions. Their versatility makes them a perfect choice for green chemistry proposals, allowing the substitution of damaging process involving hard chemical compounds or heavy energy usage. The work done focus on the better understanding of enzymatic properties and behavior to improve them for industrial application, by applying state-of-the-art modeling techniques. This knowledge has allowed the development of a new classification method for substrate promiscuity, the Effective Volume, and the design of enhanced enzyme variants. In the enzyme engineering line, this thesis presents a mutant laccase obtained through computer-aided rational design, with an improved activity over arylamines, tailored explicitly for polyaniline production. Moreover, we introduce, for the first time in our knowledge, the concept of PluriZymes, an enzyme with two fully functional active sites: an original one and a “de novo” artificially added one.<br>La producció industrial massiva generada per la nostra societat des del segle XIX, ha crescut a expenses del planeta. Els danys ambientals ja són visibles i ens animen a trobar formes de producció noves i sostenibles. Entre tots els col·laboradors, aquesta tesi es centra en els enzims i la seva possible aplicació a la indústria. Els enzims són biomolècules capaces de realitzar i accelerar les reaccions químiques. La seva versatilitat els converteix en una opció perfecta per química verda, permetent la substitució de processos nocius que comporten utilitzar compostos químics durs o un ús intensiu d’energia. Els resultats presentats es centren en una millor comprensió de les propietats enzimàtiques i del seu comportament per millorar-les per a aplicacions industrials, mitjançant l'aplicació de tècniques de modelització d'última generació. Aquest coneixement ha permès el desenvolupament d’un nou mètode de classificació de la promiscuïtat del substrat, Effective Volume, i el disseny de variants enzimàtiques millorades. En la línia d’enginyeria d’enzims, aquesta tesi presenta una lacasa mutant obtinguda a través d’un disseny racional assistit per ordinador, amb una activitat millorada sobre les arilaminas, adaptada explícitament a la producció de polianilina. A més, introduïm, per primera vegada en el nostre coneixement, el concepte de PluriZymes, un enzim amb dos llocs actius totalment funcionals, l'original i el afegit “de novo” artificial.
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He, Jingwu. "The role of yarn structure on the hand related low-stress mechanical behavior of enzyme treated yarns by Jingwu He." Thesis, Georgia Institute of Technology, 2000. http://hdl.handle.net/1853/9491.

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Books on the topic "Enzymes – Industrial applications"

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M, Linsmaier-Bednar Elfriede, ed. Industrial enzymes and their applications. Wiley, 1998.

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Bhatt, Pankaj. Industrial Applications of Microbial Enzymes. CRC Press, 2022. http://dx.doi.org/10.1201/9781003202998.

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Wolfgang, Aehle, ed. Enzymes in industry: Production and applications. 2nd ed. Wiley-VCH, 2004.

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Gerhartz, Wolfgang. Enzymes in industry: Production and applications. 2nd ed. VCH, 2004.

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Wolfgang, Gerhartz, ed. Enzymes in industry: Production and applications. VCH, 1990.

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Rotheim, Philip. The enzyme industry: Industrial and chemical applications. Business Communications Co., 1994.

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I, Laskin Allen, ed. Enzymes and immobilized cells in biotechnology. Benjamin/Cummings Pub. Co., Advanced Book Program, 1985.

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Artur, Cavaco-Paulo, Gübitz G. M, and Textile Institute, eds. Textile processing with enzymes. Woodhead Publishing, 2003.

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J, Whitehurst Robert, and Oort Maarten van, eds. Enzymes in food technology. 2nd ed. Wiley-Blackwell, 2010.

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J, Whitehurst Robert, and Law Barry A, eds. Enzymes in food technology. Sheffield Academic Press, 2002.

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Book chapters on the topic "Enzymes – Industrial applications"

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Dekker, Peter. "Dairy Enzymes." In Industrial Enzyme Applications. John Wiley & Sons, Ltd, 2019. http://dx.doi.org/10.1002/9783527813780.ch2_3.

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Østergaard, Lars H., and Hans Sejr Olsen. "Industrial Applications of Fungal Enzymes." In Industrial Applications. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-11458-8_13.

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Soccol, Carlos R., Luciana PS Vandenberghe, Adenise L. Woiciechowski, and Sumathy Babitha. "Applications of Industrial Enzymes." In Enzyme Technology. Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_27.

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Dutta, Rajiv. "Industrial Applications of Enzymes." In Fundamentals of Biochemical Engineering. Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-77901-8_4.

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Aehle, Wolfgang, and Onno Misset. "Enzymes for Industrial Applications." In Biotechnology. Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620869.ch6.

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Putseys, Joke A., and Margot E. F. Schooneveld-Bergmans. "Enzymes Used in Baking." In Industrial Enzyme Applications. John Wiley & Sons, Ltd, 2019. http://dx.doi.org/10.1002/9783527813780.ch2_1.

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de Vries, R. P., J. A. E. Benen, L. H. de Graaff, and J. Visser. "Plant Cell Wall Degrading Enzymes Produced by Aspergillus." In Industrial Applications. Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-662-10378-4_13.

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Li, Xinliang, Sandra H. Chang, and Rui Liu. "Industrial Applications of Cellulases and Hemicellulases." In Fungal Cellulolytic Enzymes. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0749-2_15.

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Rieder, Lukas, Nico Teuschler, Katharina Ebner, and Anton Glieder. "Eukaryotic Expression Systems for Industrial Enzymes." In Industrial Enzyme Applications. John Wiley & Sons, Ltd, 2019. http://dx.doi.org/10.1002/9783527813780.ch1_3.

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Hirose, Yoshihiko. "Enzymes for Human Nutrition and Health." In Industrial Enzyme Applications. John Wiley & Sons, Ltd, 2019. http://dx.doi.org/10.1002/9783527813780.ch3_1.

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Conference papers on the topic "Enzymes – Industrial applications"

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Lee, Hyeseung, Dean Ho, Benjamin Chu, Karen Kuo, and Carlo Montemagno. "Reconstituting Membrane Proteins Into Artificial Membranes and Detection of Their Activities." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46016.

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We have successfully purified BR from purple membrane of Halobacterium Salinarium and Cox from the genetically engineered plasmid inserted in Rhodobacter Sphaeroides. The activities of the purified enzymes have shown in lipid vesicles as well as in polymer vesicles and planar membranes. Phosphatidylcholine derived lipid vesicles created the most nature like environment for the enzymes. Triblock copolymer membrane was the alternative choice for membrane protein reconstitution since polymers are more durable, ideal for industrial applications and support enzyme activities better. We also demonstrated the backward function of Cox in vitro by changing proton concentration in the surrounding medium. Langmuir-Blodgett method was used to reconstitute the enzymes into the planar lipid or polymer membranes. The enzyme activities of the enzymes in planar membrane system were tested by impedance spectroscopy.
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Abd Rahim, Siti Noraida, Alawi Sulaiman, Nurul Aini Edama, et al. "Kinetic study of free and immobilized enzymes for bioconversion of tapioca slurry into BioSugar." In 2013 IEEE Business Engineering and Industrial Applications Colloquium (BEIAC). IEEE, 2013. http://dx.doi.org/10.1109/beiac.2013.6560195.

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Grushcow, J., and M. A. Smith. "Next Generation Feedstocks From New Frontiers in Oilseed Engineering." In World Tribology Congress III. ASMEDC, 2005. http://dx.doi.org/10.1115/wtc2005-63523.

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Recent advances in molecular breeding techniques along with developing tools for Genomics and Proteomics are delivering new oil seed profiles for industrial applications. Ultra high Oleic, Erucic and blends including Hydroxy fatty acids are now, or will be shortly, available in a variety of oilseed crops including Soybean and Canola as well as Flax. As a result, vegetable oils need to be re-examined by industry for specific applications. Feedstocks and base oils derived from oil seeds are renewable as well as biodegradable. A brief summary of recent progress is presented together with a description of new research into the development of an alternative source of Hydroxy fatty acids to replace castor oil and an overview of an enzyme engineering approach to create new enzymes for seed oil modification.
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Bhushan, Indu. "Efficient media for high production of microbial lipase from Bacillus subtilis (BSK-L) using response surface methodology for enantiopure synthesis of drug molecules." In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.044.

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Lipases are a multipurpose enzyme that holds a significant position in industrial applications due to its ability to catalyse a large number of reactions such as hydrolysis, esterification, interesterification, transesterification which makes it a potential candidate. It is also used for the separation of chiral drugs from the racemic mixture and this property of lipase is considered very important in pharmaceutical industries for the synthesis of enantiopure bioactive molecules. Assuming the tremendous importance of lipases, as stereoselective biocatalysts, in pharmaceuticals and various other commercial applications, industrial enzymologists have been forced to search for those microorganisms which are able to produce novel biocatalysts at reasonably high yield. In the present study microbial lipase was isolated from the water sample of pond at Katra, Jammu and Kashmir (India). This enzyme has shown wide specificity and higher enantioselectivity, which make it pharmaceutical important enzyme. To make it economical for industrial application, it was produced on cheap nutrient media using Response Surface Methodology and got maximum production. It was used for resolution of chiral drugs and the significant results obtained during the course of work shall have potential towards pharmaceutical industries.
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Alves-Pereira, I., and R. Ferreira. "Yeast stress enzymes – application of microbiology and bioinformatics for initiate high school students in environmental studies." In Proceedings of the II International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld2007). WORLD SCIENTIFIC, 2009. http://dx.doi.org/10.1142/9789812837554_0131.

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Fazlena, H., S. Norsuraya, and S. N. Nadiah. "Ultrasonic assisted enzymatic reaction: An overview on ultrasonic mechanism and stability-activity of the enzyme." In 2013 IEEE Business Engineering and Industrial Applications Colloquium (BEIAC). IEEE, 2013. http://dx.doi.org/10.1109/beiac.2013.6560256.

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Topakas, Evangelos, Anastasia Zerva, and Nikolaos Tsafantakis. "Greek Basidiomycete Wild Strains for the Production of Bioactive Compounds and Enzymes with Applications in Cosmetic and Biocatalysis Industries." In 1st International Electronic Conference on Catalysis Sciences. MDPI, 2020. http://dx.doi.org/10.3390/eccs2020-07561.

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Chandrinou, Chrysoula, Dimitra Mandala, George Tsekenis, Dionysios Soulis, and Ioanna Zergioti. "Direct enzyme immobilization on SPEs for electrochemical pesticide detection in olive oil, utilizing laser induced forward transfer." In Frontiers in Ultrafast Optics: Biomedical, Scientific, and Industrial Applications XXI, edited by Peter R. Herman, Michel Meunier, and Roberto Osellame. SPIE, 2021. http://dx.doi.org/10.1117/12.2578245.

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Zhu, S. S., and Z. Q. Miao. "Dynamic Model of Paclitaxel Biosynthesis Suggests That the Key Enzyme Is Taxadiene 5alpha-Hydroxylase in Taxuschinensis Cell Suspension Culture." In International Conference on Computer Information Systems and Industrial Applications. Atlantis Press, 2015. http://dx.doi.org/10.2991/cisia-15.2015.195.

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Khanzode, Anand U., and Sachin R. Karale. "Overview of Solar Air Drying Systems in India and His Vision of Future Developments." In ASME 2006 International Solar Energy Conference. ASMEDC, 2006. http://dx.doi.org/10.1115/isec2006-99116.

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Solar Air Drying is one of the oldest method of food preservation. For several thousand years people have been preserving grapes, herbs, Potato’s, corn, milk, fruits, vegetables, spices, meat and fish by drying. Until canning was developed at the end of the 18th century, drying was virtually the only method of food preservation. It is still the most widely used method. Solar Drying is an excellent way to preserve food and solar food dryers are an appropriate food preservation technology for a sustainable world. This technology makes it possible to dehydrate and preserve food professionally without compromising on quality, color, texture, enzymes, vitamins, taste and nutritional values of foods in the process. Food scientists have found that by reducing the moisture content of food to between 10 and 20%, bacteria, yeast, mold and enzymes are all prevented from spoiling it. India is blessed with an abundance of sunlight, water and biomass. Vigorous efforts during the past two decades are now bearing fruit as people in all walks of life are more aware of the benefits of renewable energy, especially solar energy in villages and in urban or semi-urban centers of India. Industries that can benefit from application of solar energy to heat air are Food, Textiles, Dairies, Pharma and Chemical. This paper reviews the present scenario of Solar Air Dryer and strategies for future developments in India.
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