Biocatalytic Applications in Biotechnology
At present, the increasing demand for novel biotechnological products is supported through the continuous development of biocatalytic applications. As a consequence, the progress of research regarding enzymatic catalysis in aqueous, non-aqueous, organic (polar or non-polar), and/or non-solvent media...
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Format: | Electronic Book Chapter |
Language: | English |
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Basel
MDPI - Multidisciplinary Digital Publishing Institute
2023
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Online Access: | DOAB: download the publication DOAB: description of the publication |
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100 | 1 | |a Papamichael, Emmanuel M. |4 edt | |
700 | 1 | |a Stergiou, Panagiota-Yiolanda |4 edt | |
700 | 1 | |a Papamichael, Emmanuel M. |4 oth | |
700 | 1 | |a Stergiou, Panagiota-Yiolanda |4 oth | |
245 | 1 | 0 | |a Biocatalytic Applications in Biotechnology |
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520 | |a At present, the increasing demand for novel biotechnological products is supported through the continuous development of biocatalytic applications. As a consequence, the progress of research regarding enzymatic catalysis in aqueous, non-aqueous, organic (polar or non-polar), and/or non-solvent media is decisive. Experimental design methods, which also may comprise in silico studies, the design of specific reactors and conditions, the reactions of significant chemical and/or biochemical processes that are relevant to industrial production, enzyme kinetic methods, the investigation of enzymatic mechanisms and the use of immobilized enzymes and/or microbial cells on various inert matrices, are all useful. A plethora of enzymes of several classes, which may potentially be used as biocatalysts in biotechnological applications, are available. Among these enzymes, the more common are oxidoreductases (laccase, catalase, glucose oxidase, etc.), hydrolases (amylases, lipases, proteases, amidases, cellulases, esterases, etc.), isomerases (epimerases, topoisomerases, mutases, etc.), and others. By means of the aforementioned biocatalysts and the utilization of specific biotechnological methods, important, cost-effective, sustainable, and environmentally friendly processes have been applied for the synthesis and/or the conversion of a huge number of market-required products. | ||
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546 | |a English | ||
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650 | 7 | |a Biology, life sciences |2 bicssc | |
653 | |a Endoglucanese I | ||
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653 | |a Trichoderma reesei | ||
653 | |a Swapping | ||
653 | |a Protein Engineering | ||
653 | |a divalent metal ion | ||
653 | |a (R)-2-chloro-1-(2,4-dichlorophenyl) ethanol | ||
653 | |a whole-cell catalysis | ||
653 | |a Acinetobacter sp. | ||
653 | |a isolation | ||
653 | |a (R)-miconazole | ||
653 | |a G-quadruplex | ||
653 | |a DNAzymes | ||
653 | |a peroxidase | ||
653 | |a multimers | ||
653 | |a synergism | ||
653 | |a phosphotriestease | ||
653 | |a structure | ||
653 | |a function or reaction | ||
653 | |a biotechnological application | ||
653 | |a marine chitinous by-products | ||
653 | |a Paenibacillus | ||
653 | |a protease | ||
653 | |a shrimp heads | ||
653 | |a methane | ||
653 | |a methanotrophs | ||
653 | |a secondary metabolites | ||
653 | |a isoprenoid | ||
653 | |a metabolic engineering | ||
653 | |a enzyme catalysis | ||
653 | |a optimal design | ||
653 | |a process intensification | ||
653 | |a elementary process functions | ||
653 | |a benzaldehyde lyase | ||
653 | |a 2-hydroxy ketones | ||
653 | |a uricase | ||
653 | |a Vitreoscilla hemoglobin | ||
653 | |a bifunctional enzyme | ||
653 | |a uric acid | ||
653 | |a colorimetric detection | ||
653 | |a laccase | ||
653 | |a polyamide 4 | ||
653 | |a enzyme immobilization | ||
653 | |a magnetic enzyme supports | ||
653 | |a enzyme decolorization | ||
653 | |a direct linear plot | ||
653 | |a median method | ||
653 | |a product inhibition | ||
653 | |a kinetic constants | ||
653 | |a non-parametric | ||
653 | |a distribution-free method | ||
653 | |a immobilisation | ||
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653 | |a membranes | ||
653 | |a bisphenol A | ||
653 | |a environmental toxicity | ||
653 | |a erythritol | ||
653 | |a pentaerythritol | ||
653 | |a tetraesters | ||
653 | |a fatty acids | ||
653 | |a Candida antarctica lipase-B | ||
653 | |a low calorie dietary foods | ||
653 | |a biocatalysis | ||
653 | |a transaminases | ||
653 | |a enzyme stability | ||
653 | |a organic solvent | ||
653 | |a enzyme activation | ||
653 | |a lipolytic enzymes | ||
653 | |a metagenome | ||
653 | |a family V | ||
653 | |a esterification | ||
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653 | |a rhododendrol | ||
653 | |a cytochrome P450 | ||
653 | |a tyrosinase | ||
653 | |a biocatalyst | ||
653 | |a hydroxylation | ||
653 | |a bioconversion | ||
856 | 4 | 0 | |a www.oapen.org |u https://mdpi.com/books/pdfview/book/6577 |7 0 |z DOAB: download the publication |
856 | 4 | 0 | |a www.oapen.org |u https://directory.doabooks.org/handle/20.500.12854/96632 |7 0 |z DOAB: description of the publication |