Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Albinism in Africa: Historical, Geographic, Medical, Genetic, and Psychosocial Aspects provides the first in-depth reference for understanding and treating patients of human albinism in Africa. Leading international contributors examine the historical, geographic, psychosocial, genetic and molecular considerations of importance in effectively and sensitively managing this genetic disorder. Foundational chapters covering the historical and psychosocial aspects of albinism are supplemented by discussions of the pathobiology of the disease, as well as a thorough analysis of the genetics of skin pigmentation, eye pigmentation, hair pigmentation, and incidents of skin cancer involved in the manifestations of this disorder. New prenatal diagnostics and genetic testing methods, genetic risk assessment for individuals, families, and communities, and novel genetic markers that may be used for developing new therapeutics for treating albinism are also discussed in detail. The book provides care management approaches that may be applied to instances of albinism in other regions, along with guiding principles for treating rare genetic disorders and stigmatized patient populations across the globe.

Pigmentation disorders. --- Albinos and albinism --- Albinism. --- Genetics, Medical. --- Medical Genetics --- Anthropology, Physical --- Chromosome Disorders --- Sex Chromosome Disorders --- Genetic Diseases, Inborn --- Molecular Medicine --- Monophenol Monooxygenase --- Albinism --- Leucoderma --- Leucopathy --- Pigmentation disorders --- Deficiency diseases --- Metabolism --- Skin --- Disorders --- Diseases --- Africa. --- Eastern Hemisphere

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today?truly an essential publication for researchers in all fields of life sciences.Key Features* Human Genomics and Genetics* Structure and Mechanism* Regulation of Expr

Cytochrome P-450 Enzyme System. --- Cytochromes --- Mixed Function Oxygenases --- Enzymes and Coenzymes --- Oxygenases --- Hemeproteins --- Oxidoreductases --- Chemicals and Drugs --- Proteins --- Enzymes --- Amino Acids, Peptides, and Proteins --- Cytochrome P-450 Enzyme System --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- CYP450 Family --- CYP450 Superfamily --- Cytochrome P-450 Enzymes --- Cytochrome P-450 Families --- Cytochrome P-450 Monooxygenase --- Cytochrome P-450 Oxygenase --- Cytochrome P-450 Superfamily --- Cytochrome P450 --- Cytochrome P450 Superfamily --- Cytochrome p450 Families --- P-450 Enzymes --- P450 Enzymes --- Cytochrome P-450 --- Cytochrome P-450-Dependent Monooxygenase --- Cytochrome P 450 --- Cytochrome P 450 Dependent Monooxygenase --- Cytochrome P 450 Enzyme System --- Cytochrome P 450 Enzymes --- Cytochrome P 450 Families --- Cytochrome P 450 Monooxygenase --- Cytochrome P 450 Oxygenase --- Cytochrome P 450 Superfamily --- Enzymes, Cytochrome P-450 --- Enzymes, P-450 --- Enzymes, P450 --- Monooxygenase, Cytochrome P-450 --- Monooxygenase, Cytochrome P-450-Dependent --- P 450 Enzymes --- P-450 Enzymes, Cytochrome --- Superfamily, CYP450 --- Superfamily, Cytochrome P-450 --- Superfamily, Cytochrome P450 --- Biocatalysts --- Molecular Mechanisms of Pharmacological Action --- Gene Products, Protein --- Gene Proteins --- Protein Gene Products --- Proteins, Gene --- Dehydrogenase --- Oxidase --- Reductase --- Dehydrogenases --- Oxidases --- Reductases --- Heme Protein --- Heme Proteins --- Protein, Heme --- Proteins, Heme --- Coenzymes and Enzymes --- Mixed Function Oxidases --- Hydroxylases --- Monooxygenases --- Oxidases, Mixed Function --- Oxygenases, Mixed Function --- Cytochrome --- Cytochrome P-450 Enzyme --- P-450 Enzyme --- P450 Enzyme --- Cytochrome P 450 Enzyme --- Enzyme, Cytochrome P-450 --- Enzyme, P-450 --- Enzyme, P450 --- P 450 Enzyme --- P-450 Enzyme, Cytochrome --- Biocatalyst --- Enzyme --- Protein --- Oxidoreductase --- Hemeprotein --- Oxygenase --- Hydroxylase --- Mixed Function Oxidase --- Mixed Function Oxygenase --- Monooxygenase --- Function Oxidase, Mixed --- Function Oxygenase, Mixed --- Oxidase, Mixed Function --- Oxygenase, Mixed Function --- Metalloenzymes --- Enzymology --- Cytochrome p-450 --- Microsomes --- Basic Sciences. Chemistry --- Cytochrome P-450. --- Biochemistry --- Proteins and Enzymes. --- analysis.

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Biocatalysis is very appealing to the industry because it allows, in principle, the synthesis of products not accessible by chemical synthesis. Enzymes are very effective, as are precise biocatalysts, as they are enantioselective, with mild reaction conditions and green chemistry. Biocatalysis is currently widely used in the pharmaceutical industry, food industry, cosmetic industry, and textile industry. This includes enzyme production, biocatalytic process development, biotransformation, enzyme engineering, immobilization, the synthesis of fine chemicals and the recycling of biocatalysts. One of the most challenging problems in biocatalysis applications is process optimization. This Special Issue shows that an optimized biocatalysis process can provide an environmentally friendly, clean, highly efficient, low cost, and renewable process for the synthesis and production of valuable products. With further development and improvements, more biocatalysis processes may be applied in the future.

Research & information: general --- catechin --- degalloylation --- flavonol --- glycoside hydrolase --- optimization --- tannase --- immobilized DERA --- statin side chain --- continuous flow synthesis --- alginate-luffa matrix --- design of experiments --- Anguilla marmorata --- eel protein hydrolysates --- functional properties --- herbal eel extracts --- agarose --- agarase --- agarotriose --- agaropentaose --- expression --- calycosin --- calycosin-7-O-β-D-glucoside --- glucosyltransferase --- sucrose synthase --- UDP-glucose recycle --- UGT–SuSy cascade reaction --- Candida antarctica lipase A --- surface-display system --- shear rate --- mass transfer rate --- enzymatic kinetic study --- enzymatic synthesis --- β-amino acid esters --- microreactor --- aromatic amines --- Michael addition --- kraft pulp --- cellulose --- xylan --- enzymatic hydrolysis --- Penicillium verruculosum --- glucose --- xylose --- lipase --- acidolysis --- docosahexaenoic acid ethyl ester --- eicosapentaenoic acid ethyl ester --- ethyl acetate --- kinetics --- styrene monooxygenase --- indole monooxygenase --- two-component system --- chiral biocatalyst --- solvent tolerance --- biotransformation --- epoxidation --- NAD(P)H-mimics --- superoxide dismutase (SOD) --- catalase (CAT) --- glutathione reductase (GR) --- aluminum (Al) --- selenium (Se) --- mouse --- brain --- liver --- phosphatidylcholine --- 3,4-dimethoxycinnamic acid --- enzymatic interesterification --- biocatalysis --- Pleurotus ostreatus --- enenzymatic hydrolysis --- peptide --- antioxidant --- hepatoprotective activity --- Yarrowia lipolytica --- whole–cell biocatalysis --- indolizine --- cycloaddition --- trehalose --- viscosity --- enzymes --- protein dynamics --- Kramers’ theory --- protein stabilization --- enzyme inhibition --- Lipase --- transesterification --- 2-phenylethyl acetate --- packed-bed reactor --- solvent-free --- cyclic voltammetry --- electrochemical impedance spectroscopy --- carbon nanotubes --- redox mediators --- CYP102A1 --- naringin dihydrochalcone --- neoeriocitrin dihydrochalcone --- regioselective hydroxylation --- n/a --- UGT-SuSy cascade reaction --- whole-cell biocatalysis --- Kramers' theory

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Biotransformation has accompanied mankind since the Neolithic community, when people settled down and began to engage in agriculture. Modern biocatalysis started in the mid-1850s with the pioneer works of Pasteur. Today, biotransformations have become an indispensable part of our lives, similar to other hi-tech products. Now, in 2019, biocatalysis “received” the Nobel Prize in Chemistry due to prof. Frances H. Arnold’s achievements in the area of the directed evolution of enzymes. This book deals with some major topics of biotransformation, such as the application of enzymatic methods in glycobiology, including the synthesis of hyaluronan, complex glycoconjugates of N-acetylmuramic acid, and the enzymatic deglycosylation of rutin. Enzymatic redox reactions were exemplified by the enzymatic synthesis of indigo from indole, oxidations of β-ketoesters and the engineering of a horse radish peroxidase. The enzymatic reactions were elegantly employed in biosensors, such as glucose oxidase, in the case of electrochemical glucose sensors. Nitrilases are important enzymes for nitrile metabolism in plants and microorganisms have already found broad application in industry—here, these enzymes were for the first time described in Basidiomyceta. This book nicely describes molecular biocatalysis as a pluripotent methodology—“A jack of all trades...”—which strongly contributes to the high quality and sustainability of our daily lives.

Technology: general issues --- E. coli --- recombinant horseradish peroxidase --- site-directed mutagenesis --- periplasm --- glycosylation sites --- Aspergillus niger --- quercetin --- rutin --- rutinose --- rutinosidase --- “solid-state biocatalysis” --- hyaluronic acid --- in vitro synthesis --- one-pot multi-enzyme --- optimization --- enzyme cascade --- Basidiomycota --- Agaricomycotina --- nitrilase --- cyanide hydratase --- nitrile --- substrate specificity --- overproduction --- homology modeling --- substrate docking --- phylogenetic distribution --- indigo --- MISO library --- flavin --- monooxygenase --- FMO --- β-N-acetylhexosaminidases --- transglycosylation --- Glide docking --- Talaromyces flavus --- muramic acid --- non-reducing carbohydrate --- glucose oxidase --- direct electron transfer --- amine-reactive phenazine ethosulfate --- glucose sensor --- glycemic level monitoring --- Pseudomonas putida MnB1 --- biogenic manganese oxides --- abiotic manganese oxides --- α-Hydroxy-β-keto esters --- whole-cell biocatalysis --- surface display --- cell wall anchor --- Lactobacillus plantarum --- whole-cell biocatalyst --- n/a --- Fe(II)/2-ketoglutarate-dependent dioxygenase --- 2-ketoglutarate generation --- regio- and stereo-selective synthesis --- hydroxy amino acids --- sequential cascade reaction --- "solid-state biocatalysis"

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Biotransformation has accompanied mankind since the Neolithic community, when people settled down and began to engage in agriculture. Modern biocatalysis started in the mid-1850s with the pioneer works of Pasteur. Today, biotransformations have become an indispensable part of our lives, similar to other hi-tech products. Now, in 2019, biocatalysis “received” the Nobel Prize in Chemistry due to prof. Frances H. Arnold’s achievements in the area of the directed evolution of enzymes. This book deals with some major topics of biotransformation, such as the application of enzymatic methods in glycobiology, including the synthesis of hyaluronan, complex glycoconjugates of N-acetylmuramic acid, and the enzymatic deglycosylation of rutin. Enzymatic redox reactions were exemplified by the enzymatic synthesis of indigo from indole, oxidations of β-ketoesters and the engineering of a horse radish peroxidase. The enzymatic reactions were elegantly employed in biosensors, such as glucose oxidase, in the case of electrochemical glucose sensors. Nitrilases are important enzymes for nitrile metabolism in plants and microorganisms have already found broad application in industry—here, these enzymes were for the first time described in Basidiomyceta. This book nicely describes molecular biocatalysis as a pluripotent methodology—“A jack of all trades...”—which strongly contributes to the high quality and sustainability of our daily lives.

E. coli --- recombinant horseradish peroxidase --- site-directed mutagenesis --- periplasm --- glycosylation sites --- Aspergillus niger --- quercetin --- rutin --- rutinose --- rutinosidase --- “solid-state biocatalysis” --- hyaluronic acid --- in vitro synthesis --- one-pot multi-enzyme --- optimization --- enzyme cascade --- Basidiomycota --- Agaricomycotina --- nitrilase --- cyanide hydratase --- nitrile --- substrate specificity --- overproduction --- homology modeling --- substrate docking --- phylogenetic distribution --- indigo --- MISO library --- flavin --- monooxygenase --- FMO --- β-N-acetylhexosaminidases --- transglycosylation --- Glide docking --- Talaromyces flavus --- muramic acid --- non-reducing carbohydrate --- glucose oxidase --- direct electron transfer --- amine-reactive phenazine ethosulfate --- glucose sensor --- glycemic level monitoring --- Pseudomonas putida MnB1 --- biogenic manganese oxides --- abiotic manganese oxides --- α-Hydroxy-β-keto esters --- whole-cell biocatalysis --- surface display --- cell wall anchor --- Lactobacillus plantarum --- whole-cell biocatalyst --- n/a --- Fe(II)/2-ketoglutarate-dependent dioxygenase --- 2-ketoglutarate generation --- regio- and stereo-selective synthesis --- hydroxy amino acids --- sequential cascade reaction --- "solid-state biocatalysis"