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This book discusses biochemical adaptation to environments from freezing polar oceans to boiling hot springs, and under hydrostatic pressures up to 1,000 times that at sea level.Originally published in 1984.The Princeton Legacy Library uses the latest print-on-demand technology to again make available previously out-of-print books from the distinguished backlist of Princeton University Press. These editions preserve the original texts of these important books while presenting them in durable paperback and hardcover editions. The goal of the Princeton Legacy Library is to vastly increase access to the rich scholarly heritage found in the thousands of books published by Princeton University Press since its founding in 1905.

Adaptation (Physiology) --- Biochemistry. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Compensation (Physiology) --- Plasticity (Physiology) --- Composition --- Biology --- Chemistry --- Medical sciences --- Ecophysiology --- Biochemistry --- 57.017.32 --- 575.826 --- 575.826 Adaptation --- Adaptation --- Biologische wetenschappen in het algemeen. Biologie--?.017.32 --- 6-bisphosphatase. --- ATPase. --- Acid–base homeostasis. --- Adenosine monophosphate. --- Alanine. --- Alcohol dehydrogenase. --- Amino acid. --- Aminooxyacetic acid. --- Anabolism. --- Anaerobic glycolysis. --- Antifreeze. --- Arginine. --- Basal rate. --- Beta oxidation. --- Bohr effect. --- Carbohydrate. --- Carnitine. --- Catabolism. --- Catalase. --- Catalysis. --- Cellular respiration. --- Cofactor (biochemistry). --- Competitive inhibition. --- Cooperativity. --- Deep sea. --- Dehydrogenase. --- Detergent. --- Dissociation constant. --- Enzyme Repression. --- Enzyme inhibitor. --- Enzyme. --- Facultative anaerobic organism. --- Fatty acid. --- Fermentation. --- Flavin adenine dinucleotide. --- Fructose 1. --- Futile cycle. --- Glucagon. --- Gluconeogenesis. --- Glucose-6-phosphate dehydrogenase. --- Glucose. --- Glyceraldehyde 3-phosphate dehydrogenase. --- Glycerol. --- Glycogen phosphorylase. --- Glycogen. --- Glycogenolysis. --- Glycolysis. --- Hemoglobin. --- Hibernation. --- High-energy phosphate. --- Hill equation (biochemistry). --- Histidine. --- Hofmeister series. --- Hormone-sensitive lipase. --- Insulin. --- Isozyme. --- Ketosis. --- Lactic acid. --- Lipid. --- Lipolysis. --- Lysine. --- Mammalian diving reflex. --- Metabolic intermediate. --- Metabolism. --- Michaelis–Menten kinetics. --- Mitochondrial matrix. --- Mitochondrion. --- Molecular mimicry. --- Muscle. --- Nicotinamide adenine dinucleotide. --- Obligate anaerobe. --- Obligate. --- Organism. --- Ornithine. --- Osmolyte. --- Oxidative deamination. --- Peroxidase. --- Phosphagen. --- Phosphofructokinase. --- Phospholipid. --- Phosphorylase kinase. --- Proline. --- Proofreading (biology). --- Protein turnover. --- Protein. --- Proteolysis. --- Pyruvate carboxylase. --- Pyruvic acid. --- Redox. --- Regulatory enzyme. --- Root effect. --- Substrate-level phosphorylation. --- Thermoregulation. --- Thermus aquaticus. --- Thermus thermophilus. --- Triglyceride. --- Tryptophan. --- Turnover number. --- Urea cycle. --- Urea.

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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

Choose an application

• Reference Manager
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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