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1. Full Text Federal and private roles in the development and provision of alglucerase therapy for Gaucher disease
by Garber, Alan M and United States. Congress.Office of Technology Assessment
1992, Background paper, ISBN 0160381290
Orphan drugs | Orphan Drug Production | economics | Treatment | drug therapy | Pharmaceutical policy | United States | Glucosylceramidase | Gaucher Disease | therapeutic use | Gaucher's disease
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2. Full Text Beta-glucosidase 1 (GBA1) is a second bile acid β-glucosidase in addition to β-glucosidase 2 (GBA2). Study in β-glucosidase deficient mice and humans
by Harzer, Klaus and Blech-Hermoni, Yotam and Goldin, Ehud and Felderhoff-Mueser, Ursula and Igney, Claudia and Sidransky, Ellen and Yildiz, Yildiz
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 06/2012, Volume 423, Issue 2, pp. 308 - 312
► Lysosomal glucosylceramidase (beta-glucosidase 1, GBA1) is in addition to the non-lysosomal glucosylceramidase (beta-glucosidase 2, GBA2) a second bile acid... 
Glucosylceramide lipidosis | β-Glucosidase 1 | β-Glucosidase 2 (GBA2) | β-Glucosidase null mice | GBA1 | Isofagomine | Bile acid β-glucosidases | beta-Glucosidase null mice | beta-Glucosidase 2 (GBA2) | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | BETA-GLUCOSIDASE-2 | GLUCOCEREBROSIDASE | BIOPHYSICS | TYPE-2 GAUCHER-DISEASE | PURIFICATION | MUTATION | beta-Glucosidase 1 (GBA1) | ACCUMULATION | Bile acid beta-glucosidases | HUMAN-LIVER | Fibroblasts - enzymology | Liver - enzymology | Humans | Bile Acids and Salts - chemistry | Brain - enzymology | Bile Acids and Salts - metabolism | Male | Glucosides - metabolism | beta-Glucosidase - chemistry | Hydrolysis | Animals | beta-Glucosidase - genetics | Glucosides - chemistry | beta-Glucosidase - metabolism | Mice | Gaucher Disease - enzymology | Index Medicus | β-Glucosidase 1 (GBA1)
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3. Full Text Comparative phenomics and targeted use of genomics reveals variation in carbon and nitrogen assimilation among different Brettanomyces bruxellensis strains
by Crauwels, S and Van Assche, A and de Jonge, R and Borneman, A R and Verreth, C and Troels, P and De Samblanx, G and Marchal, K and Van de Peer, Y and Willems, K A and Verstrepen, K J and Curtin, C D and Lievens, B
Applied Microbiology and Biotechnology, ISSN 0175-7598, 11/2015, Volume 99, Issue 21, pp. 9123 - 9134
Recent studies have suggested a correlation between genotype groups of Brettanomyces bruxellensis and their source of isolation. To further explore this... 
Life Sciences | Biotechnology | Dekkera bruxellensis | β-Glucosidase | Microbiology | α-Glucosidase | Microbial Genetics and Genomics | Biolog | Phenotypic and genetic diversity | Niche adaptation | WINE | DEKKERA-BRUXELLENSIS | IDENTIFICATION | BEER | GENETIC DIVERSITY | YEAST ECOLOGY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | beta-Glucosidase | alpha-Glucosidase | FERMENTATION | CIDER | Wine - microbiology | Brettanomyces - genetics | Carbon - metabolism | Sequence Deletion | Nitrogen - metabolism | DNA, Fungal - genetics | Genomics | Brettanomyces - classification | Genotype | Beer - microbiology | Genetic Variation | alpha-Glucosidases - genetics | Metabolic Networks and Pathways - genetics | Phenotype | beta-Glucosidase - genetics | Polymerase Chain Reaction | beta-Glucosidase - metabolism | Brettanomyces - physiology | Brettanomyces - isolation & purification | Carbonated Beverages - microbiology | alpha-Glucosidases - metabolism | Influence | Research | Beverages | Sugars | Monosaccharides | Studies | Genotype & phenotype | Genetic diversity | Yeast | Analysis | Index Medicus
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4. Full Text Adsorption of enzyme onto lignins of liquid hot water pretreated hardwoods
by Ko, Ja Kyong and Ximenes, Eduardo and Kim, Youngmi and Ladisch, Michael R
Biotechnology and Bioengineering, ISSN 0006-3592, 03/2015, Volume 112, Issue 3, pp. 447 - 456
Addition of BSA doubles enzyme hydrolysis of cellulose but has little effect on hydrolysis of Avicel at cellulase loading of 5 FPU/g glucan. 
adsorption | lignin | β‐glucosidase | liquid hot water pretreatment | enzymatic hydrolysis | cellulase | Lignin | Adsorption | β-glucosidase | Cellulase | Enzymatic hydrolysis | Liquid hot water pretreatment | glucosidase | BIOFUEL PRODUCTION | TRICHODERMA-REESEI | HYDROLYSIS | CELLOBIOHYDROLASE-I | INHIBITION | POLY(ETHYLENE GLYCOL) | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PURIFICATION | BETA-GLUCOSIDASE | SOFTWOOD | Cellulase - chemistry | Fungal Proteins - chemistry | Water | Sodium Chloride | Lignin - chemistry | Hot Temperature | beta-Glucosidase - chemistry | Hydrolysis | Cellulase - metabolism | Lignin - metabolism | Wood - chemistry | beta-Glucosidase - metabolism | Fungal Proteins - metabolism | Enzymes | Analysis | Cellulose | Chemical properties | Bioengineering | Wood products | Electrostatics | Index Medicus | Liquids | Hardwoods
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5. Full Text High β-glucosidase (GBA) activity not attributable to GBA1 and GBA2 in live normal and enzyme-deficient fibroblasts may emphasise the role of additional GBAs
by Harzer, Klaus and Yildiz, Yildiz
Biological Chemistry, ISSN 1431-6730, 11/2015, Volume 396, Issue 11, pp. 1241 - 1246
Beta-glucosidases (GBA) include GBA1, GBA2 and other β-glucosidases (non-GBA1-2). GBA1 is a lysosomal and GBA2 an extra-lysosomal enzyme. GBA1- and... 
β-glucosidase 2 deficiency | glucosylceramide loading fibroblasts | Gaucher disease | β-glucosidase 2 | β-glucosidase 1 | glucocerebrosidase | STORAGE DISEASE | PROSAPOSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | beta-glucosidase 2 deficiency | beta-glucosidase 2 | beta-glucosidase 1 | IDENTIFICATION | GAUCHER-DISEASE | BETA-GLUCOSIDASE-2 | MUTATION | PATIENT | NONLYSOSOMAL GLUCOSYLCERAMIDASE | CULTURED FIBROBLASTS | Fibroblasts - enzymology | Humans | Child, Preschool | Fibroblasts - pathology | beta-Glucosidase - deficiency | Animals | beta-Glucosidase - genetics | beta-Glucosidase - metabolism | Mice | Enzyme Activation | Child | Infant, Newborn | Fibroblasts - metabolism | Index Medicus
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6. Full Text Interaction of antidiabetic α‐glucosidase inhibitors and gut bacteria α‐glucosidase
by Tan, Kemin and Tesar, Christine and Wilton, Rosemarie and Jedrzejczak, Robert P and Joachimiak, Andrzej and Argonne National Lab. (ANL), Argonne, IL (United States)
Protein Science, ISSN 0961-8368, 08/2018, Volume 27, Issue 8, pp. 1498 - 1508
Carbohydrate hydrolyzing α‐glucosidases are commonly found in microorganisms present in the human intestine microbiome. We have previously reported crystal... 
α‐glucosidase | α‐glucosidase inhibitor | substrate/inhibitor selection | acarbose | antidiabetic drug | voglibose | miglitol | human gut microbiome | α-glucosidase | α-glucosidase inhibitor | SITE | ANTIBIOTICS | MUTAGENESIS | alpha-glucosidase inhibitor | BIOCHEMISTRY & MOLECULAR BIOLOGY | TOXICITY | HUMAN MICROBIOME PROJECT | BIOFUELS | alpha-glucosidase | METABOLISM | inhibitor selection | DRUGS | INTESTINAL MALTASE-GLUCOAMYLASE | substrate | Binding | Carbohydrates | Acarbose | Digestive system | Diabetes mellitus | Miglitol | Microbiomes | Homology | Glucosidase | Drug development | Substrates | Microorganisms | Inhibitors | Intestine | Substrate preferences | Bacteria | Glucoamylase | Digestive tract | Crystal structure | Index Medicus | BASIC BIOLOGICAL SCIENCES | anti-diabetic drug | Full‐Length Papers
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7. Full Text Overexpression and characterization of a glucose-tolerant β-glucosidase from T. aotearoense with high specific activity for cellobiose
by Yang, Fang and Yang, Xiaofeng and Li, Zhe and Du, Chenyu and Wang, Jufang and Li, Shuang
Applied Microbiology and Biotechnology, ISSN 0175-7598, 11/2015, Volume 99, Issue 21, pp. 8903 - 8915
Thermoanaerobacterium aotearoense P8G3#4 produced β-glucosidase (BGL) intracellularly when grown in liquid culture on cellobiose. The gene bgl, encoding... 
Life Sciences | Thermoanaerobacterium aotearoense P8G3#4 | Glucose tolerance | Cellobiose degradation | Biotechnology | β-Glucosidase | Microbiology | Microbial Genetics and Genomics | Chaperones | TRICHODERMA-REESEI | ESCHERICHIA-COLI | THERMOANAEROBACTERIUM-AOTEAROENSE | CLOSTRIDIUM-CELLULOVORANS | HYDROLYSIS | SUGARCANE BAGASSE | BIOETHANOL PRODUCTION | SUBSTRATE-SPECIFICITY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | beta-Glucosidase | PURIFICATION | HYDROGEN-PRODUCTION | Potassium - metabolism | Temperature | Open Reading Frames | Molecular Sequence Data | Enzyme Activators - metabolism | Sodium - metabolism | beta-Glucosidase - chemistry | Recombinant Proteins - isolation & purification | beta-Glucosidase - genetics | Cloning, Molecular | Escherichia coli - metabolism | beta-Glucosidase - metabolism | Thermoanaerobacterium - enzymology | Recombinant Proteins - metabolism | Gene Expression | beta-Glucosidase - isolation & purification | Enzyme Inhibitors - metabolism | Enzyme Stability | Thermoanaerobacterium - genetics | Models, Molecular | Recombinant Proteins - chemistry | Cellobiose - metabolism | Recombinant Proteins - genetics | Sequence Analysis, DNA | Hydrolysis | Sequence Homology, Amino Acid | Thermoanaerobacterium - growth & development | Escherichia coli - genetics | Glucose - metabolism | Protein Conformation | Kinetics | Hydrogen-Ion Concentration | Index Medicus
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8. Full Text Purification and enzymatic characterization of a novel β-1,6-glucosidase from Aspergillus oryzae
by Watanabe, Akira and Suzuki, Moe and Ujiie, Seiryu and Gomi, Katsuya
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 03/2016, Volume 121, Issue 3, pp. 259 - 264
In this study, among the 10 genes that encode putative β-glucosidases in the glycoside hydrolase family 3 (GH3) with a signal peptide in the genome, we found a... 
β-Glucosidase | Aspergillus oryzae | β-1,6-Glucosidase | Gentiobiose | Glycoside hydrolase family 3 | SUBSTRATE-SPECIFICITY | GENE | TRANSGLYCOSYLATION ACTIVITY | CLONING | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | beta-Glucosidase | FOOD SCIENCE & TECHNOLOGY | beta-1,6-Glucosidase | GENOME | Temperature | beta-Glucosidase - isolation & purification | Disaccharides - metabolism | Enzyme Stability | Substrate Specificity | Food Industry | Hydrolysis | beta-Glucosidase - antagonists & inhibitors | Aspergillus oryzae - genetics | Aspergillus oryzae - enzymology | beta-Glucosidase - genetics | beta-Glucosidase - metabolism | Hydrogen-Ion Concentration | Index Medicus
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9. Full Text Biochemical and structural characterization of a thermostable β-glucosidase from Halothermothrix orenii for galacto-oligosaccharide synthesis
by Hassan, Noor and Nguyen, Thu-Ha and Intanon, Montira and Kori, Lokesh D and Patel, Bharat K. C and Haltrich, Dietmar and Divne, Christina and Tan, Tien Chye and Skolan för bioteknologi (BIO) and KTH
Applied Microbiology and Biotechnology, ISSN 0175-7598, 2/2015, Volume 99, Issue 4, pp. 1731 - 1744
Lactose is a major disaccharide by-product from the dairy industries, and production of whey alone amounts to about 200 million tons globally each year. Thus,... 
Life Sciences | Halothermothrix | Biotechnology | Biochemical characterization | β -glucosidase | Microbiology | Microbial Genetics and Genomics | Lactose conversion | Galacto-oligosaccharides | β -galactosidase | Halothermophile | Structural analysis | β-galactosidase | β-glucosidase | GLYCOSIDASE | beta-galactosidase | LACTOSE | ASPERGILLUS-ORYZAE | beta-glucosidase | SUBSTRATE-SPECIFICITY | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | PERSPECTIVES | PURIFICATION | BACTERIUM | INHIBITORS | TRANSGLYCOSIDASE | LACTOBACILLUS-REUTERI | Galactose - metabolism | Temperature | Enzyme Stability | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Clostridium - genetics | Oligosaccharides - biosynthesis | beta-Glucosidase - chemistry | Clostridium - enzymology | Lactose - metabolism | beta-Glucosidase - genetics | Glucose - metabolism | beta-Glucosidase - metabolism | Protein Conformation | Hydrogen-Ion Concentration | Index Medicus | Biotechnologically Relevant Enzymes and Proteins | Biological Sciences | Mikrobiologi | Naturvetenskap | Biologiska vetenskaper | Natural Sciences
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10. Full Text α- and β-Glucosidase inhibitors: chemical structure and biological activity
by Borges de Melo, Eduardo and da Silveira Gomes, Adriane and Carvalho, Ivone
Tetrahedron, ISSN 0040-4020, 2006, Volume 62, Issue 44, pp. 10277 - 10302
Glycoside trimming enzymes are crucially important in a broad range of metabolic pathways, including glycoprotein and glycolipid processing and carbohydrate... 
β-Glucosidase | Iminosugar | Carbasugar | α-Glucosidase | Non-glycosidic bond | Disaccharide | Thiosugar | Glucosidase inhibitor | LONG-TERM | CONDURITOL-A | GYMNEMA-SYLVESTRE | glucosidase inhibitor | CHEMISTRY, ORGANIC | TRANSITION-STATE | beta-glucosidase | carbasugar | iminosugar | alpha-glucosidase | non-glycosidic bond | POTENT GLYCOSIDASE INHIBITORS | SULFONIUM SULFATE STRUCTURE | MEDICINE SALACIA-RETICULATA | disaccharide | CONFORMATIONAL-ANALYSIS | thiosugar | TYPE-2 DIABETES-MELLITUS | SPONGE PENARES SP
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11. Full Text Structural Basis for Broad Substrate Specificity in Higher Plant β-D-Glucan Glucohydrolases
by Maria Hrmova and Ross De Gori and Brian J. Smith and Jon K. Fairweather and Hugues Driguez and Joseph N. Varghese and Geoffrey B. Fincher
The Plant Cell, ISSN 1040-4651, 5/2002, Volume 14, Issue 5, pp. 1033 - 1052
Family 3 β-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze the hydrolytic removal of β-D-glucosyl residues from... 
Enzymes | Barley | Active sites | Substrate specificity | Atoms | Amino acids | Kinetics | Enzyme substrates | Functional groups | Plant cells | CELLULOSE-BINDING DOMAIN | PATHOGEN INTERACTIONS | WALL-BOUND EXO-1,3-BETA-D-GLUCANASE | D-GLUCOSIDASE | TRICHODERMA-REESEI | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTAL-STRUCTURES | GLYCOSIDE HYDROLASE | PLANT SCIENCES | CELL BIOLOGY | BARLEY HORDEUM-VULGARE | CATALYTIC MECHANISM | SUBSITE AFFINITIES | Disaccharides - metabolism | Glucosidases - metabolism | Glycoside Hydrolases - genetics | Glucosidases - genetics | Molecular Sequence Data | Substrate Specificity | Structure-Activity Relationship | Phylogeny | Disaccharides - chemistry | beta-Glucosidase - chemistry | Plants - enzymology | Glucosidases - chemistry | Glucan Endo-1,3-beta-D-Glucosidase - chemistry | Trisaccharides - chemistry | Plants - genetics | beta-Glucosidase - genetics | Glucan Endo-1,3-beta-D-Glucosidase - metabolism | Glycoside Hydrolases - chemistry | beta-Glucosidase - metabolism | Glucans - metabolism | Catalysis | Trisaccharides - metabolism | Binding Sites | Carbohydrate Sequence | Amino Acid Sequence | Glucan Endo-1,3-beta-D-Glucosidase - genetics | Models, Molecular | Cellobiose - metabolism | Sequence Homology, Amino Acid | Cellobiose - chemistry | Protein Binding | Glucans - chemistry | Glycoside Hydrolases - metabolism | Index Medicus
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12. Full Text β-Glucosidase activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose
by Zanoelo, Fabiana Fonseca and Polizeli, Maria de Lourdes Teixeira de Moraes and Terenzi, Héctor Francisco and Jorge, João Atílio
FEMS Microbiology Letters, ISSN 0378-1097, 2004, Volume 240, Issue 2, pp. 137 - 143
An inducible mycelial β-glucosidase from was characterized. The enzyme exhibited a p of 6.5, a carbohydrate content of 15%, and an apparent molecular mass of... 
β-Glucosidase | Glucose-exhanced β-glucosidase | Scytalidium thermophilum | Cellobiase | β-Glycosidase | Xylose-exhanced β-glucosidase | HUMICOLA-GRISEA | MICROBIOLOGY | glucose-exhanced beta-glucosidase | beta-glucosidase | beta-glycosidase | ENZYME | ELECTROPHORESIS | CLONING | xylose-exhanced beta-glucosidase | PURIFICATION | TOLERANT | cellobiase | PROTEINS | Enzyme Activators - pharmacology | Temperature | Molecular Weight | beta-Glucosidase - isolation & purification | Nitrophenylgalactosides - metabolism | Disaccharides - metabolism | Enzyme Stability | Enzyme Induction | Substrate Specificity | Cellobiose - metabolism | Ascomycota - enzymology | Glucose - pharmacology | Glucosides - metabolism | beta-Glucosidase - chemistry | Lactose - metabolism | Glycosides - metabolism | Isoelectric Point | beta-Glucosidase - metabolism | Hydrogen-Ion Concentration | Xylose - pharmacology | Index Medicus
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13. Full Text Function and structure of GH13_31 α‐glucosidase with high α‐(1→4)‐glucosidic linkage specificity and transglucosylation activity
by Auiewiriyanukul, Waraporn and Saburi, Wataru and Kato, Koji and Yao, Min and Mori, Haruhide
FEBS Letters, ISSN 0014-5793, 07/2018, Volume 592, Issue 13, pp. 2268 - 2281
α‐Glucosidase hydrolyzes α‐glucosides and transfers α‐glucosyl residues to an acceptor through transglucosylation. In this study, GH 13_31 α‐glucosidase Bsp AG... 
α‐glucosidase | transglycosylation | glycoside hydrolase family 13 | α-glucosidase | DEXTRAN GLUCOSIDASE | STREPTOCOCCUS-MUTANS | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYCOSIDE HYDROLASE FAMILY-13 | CELL BIOLOGY | alpha-glucosidase | BIOPHYSICS | ALIGNMENT | ENZYMES | SUBSTRATE RECOGNITION MECHANISM | SEQUENCE | INHIBITOR | BINDING | Amino Acid Sequence | Mutagenesis, Site-Directed | Catalytic Domain - genetics | Carbohydrate Metabolism - genetics | Carbohydrate Sequence - physiology | Models, Molecular | Bacillus - genetics | Glycosylation | Structure-Activity Relationship | Substrate Specificity - genetics | Glucosides - metabolism | Hydrolysis | alpha-Glucosidases - genetics | Bacillus - enzymology | Glucosides - chemistry | Kinetics | alpha-Glucosidases - metabolism | alpha-Glucosidases - chemistry | Index Medicus
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