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EPIDERMIS --- KERATIN --- EPIDERMIS --- KERATIN

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Keratin. --- Molecular structure. --- Histology. --- Histology --- Evolution --- Extraction --- Keratins

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This book provides information about the sources, structure, and properties of keratin as well as its applications. The extraction from different biomass sources (e.g. feathers, hairs, nails, horn, hoof, and claws) as well as the characterization methods of these extracted materials are explained. The development of bioproducts from keratins is challenging and limited since they are neither soluble in polar solvents nor in non-polar solvents. Therefore, the utilization of different microorganisms for the degradation of keratin is also discussed. The main aim of this book is to highlight the unique features of keratin and to update readers with the possible prospects to develop various value-added products from keratins. The book is highly interesting to researchers working in industry and academia on bioproducts, tissue engineering, biocomposites, biofilm, and biofibers.

Biopolymers --- Keratin. --- Biotechnology. --- Polymers. --- Sustainable development. --- Biochemical engineering. --- Environmental chemistry. --- Bioorganic chemistry. --- Polymer Sciences. --- Sustainable Development. --- Biochemical Engineering. --- Environmental Chemistry. --- Bioorganic Chemistry. --- Bio-organic chemistry --- Biological organic chemistry --- Biochemistry --- Chemistry, Organic --- Chemistry, Environmental --- Chemistry --- Ecology --- Bio-process engineering --- Bioprocess engineering --- Biotechnology --- Chemical engineering --- Development, Sustainable --- Ecologically sustainable development --- Economic development, Sustainable --- Economic sustainability --- ESD (Ecologically sustainable development) --- Smart growth --- Sustainable development --- Sustainable economic development --- Economic development --- Polymere --- Polymeride --- Polymers and polymerization --- Macromolecules --- Environmental aspects --- Polymers  .

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The concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for “green” synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications.

Technology: general issues --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals --- 2G ethanol --- hemicellulose usage --- S. cerevisiae --- enzyme immobilization --- cell immobilization --- SHIF --- mannonate dehydratase --- mannose metabolism --- Thermoplasma acidophilum --- mannono-1,4-lactone --- 2-keto-3-deoxygluconate --- aldohexose dehydrogenase --- cyclodextrin glucanotransferases --- large-ring cyclodextrins --- semi rational mutagenesis --- carbohydrate active enzymes --- archaea --- glycosidase --- Sulfolobus solfataricus --- Saccharolobus solfataricus --- Lactobacillus --- β-galactosidase --- immobilization --- cell surface display --- LysM domains --- biocatalysis --- extremophile --- 5-hydroxymethylfurfural --- 5-hydroxymethylfuroic acid --- platform chemicals --- whole cells --- New Delhi metallo-β-lactamase --- NDM-24 --- kinetic profile --- secondary structure --- glycoside hydrolase --- thioglycosides --- Fervidobacterium --- endo-β-1,3-glucanase --- laminarinase --- thermostable --- gene duplication --- cofactor F420 --- deazaflavin --- oxidoreductase --- hydride transfer --- hydrogenation --- asymmetric synthesis --- cofactor biosynthesis --- ω-transaminase --- α-methylbenzylamine --- chiral amine --- biotransformation --- biodiesel --- waste cooking oil --- lipase immobilization --- interfacial activation --- functionalized magnetic nanoparticles --- DNase --- kinetic profiles --- RNase --- semi-rational mutagenesis --- substrate specificity --- engineered Escherichia coli --- flavonoid glucuronides --- multienzyme whole-cell biocatalyst --- organic solvents --- psychrophilic yeast --- hormone-sensitive lipase --- Glaciozyma antarctica --- Antarctica and homology modelling --- keratinase --- serine protease --- metalloprotease --- peptidase --- keratin hydrolysis --- keratin waste --- valorisation --- bioactive peptides --- ene reductase --- enzyme sourcing --- old yellow enzyme --- solvent stability --- machine learning --- flux optimization --- artificial neural network --- synthetic biology --- glycolysis --- metabolic pathways optimization --- cell-free systems --- hydrolase --- lipase --- esterase --- Bacillus subtilis lipase A --- transesterification --- organic solvent --- water activity --- immobilized lipase --- RSM --- fuel properties --- chemo-enzymatic synthesis --- glycosyl transferases --- protein engineering --- carbohydrates --- industrial enzymes --- thermostable enzymes --- glycoside hydrolases --- cell-free biocatalysis --- natural and non-natural multi-enzyme pathways --- bio-based chemicals