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1. Full Text Structural basis for enzyme bifunctionality – the case of Gan1D from Geobacillus stearothermophilus
by Lansky, Shifra and Zehavi, Arie and Belrhali, Hassan and Shoham, Yuval and Shoham, Gil
The FEBS journal, ISSN 1742-464X, 11/2017, Volume 284, Issue 22, pp. 3931 - 3953
negative cooperativity | 6‐phospho‐β‐glucosidase | galactan utilization | structure‐function relationships | 6‐phospho‐β‐galactosidase | semi‐conservative resolution cut‐off | small‐angle X‐ray scattering | broad specificity | 6-phospho-β-galactosidase | 6-phospho-β-glucosidase | structure-function relationships | semi-conservative resolution cut-off | small-angle X-ray scattering | Amino Acid Sequence | Catalytic Domain | Geobacillus stearothermophilus - enzymology | Glucosidases - metabolism | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Glucosidases - chemistry | Sequence Homology | Phosphates - metabolism | Glycoside Hydrolases - chemistry | Protein Conformation | Catalysis | Glycoside Hydrolases - metabolism | Binding Sites | Galactosephosphates - metabolism | Phosphates | Enzymes | Biological products | Analysis | Crystals | Galactose | Structure | Protein binding | Residues | Galactosidase | Small angle X ray scattering | X-ray scattering | Cellobiose | 6-Phospho-β-glucosidase | Atomic structure | Bioinformatics | Crystal structure | Biodegradation | Degradation products | Tertiary structure | Glucosidase | Organic chemistry | Quaternary structure | X ray scattering | Mutation | Growth hormone | Protein structure | Binding sites | Glycoside hydrolase | Structure-function relationships | Index Medicus
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2. Full Text Protein Engineering by Random Mutagenesis and Structure-Guided Consensus of Geobacillus stearothermophilus Lipase T6 for Enhanced Stability in Methanol
by Adi Dror and Einav Shemesh and Natali Dayan and Ayelet Fishman
Applied and Environmental Microbiology, ISSN 0099-2240, 02/2014, Volume 80, Issue 4, pp. 1515 - 1527
Life Sciences & Biomedicine | Microbiology | Biotechnology & Applied Microbiology | Science & Technology | Solvents | Geobacillus stearothermophilus - enzymology | Enzyme Inhibitors - metabolism | Protein Engineering - methods | Enzyme Stability | Mutant Proteins - genetics | Models, Molecular | Mutant Proteins - metabolism | Geobacillus stearothermophilus - genetics | Lipase - metabolism | Lipase - chemistry | Molecular Dynamics Simulation | Methanol - metabolism | Mutagenesis | Mutant Proteins - chemistry | Amino Acid Substitution | Lipase - genetics | Protein engineering | Gram-positive bacteria | Physiological aspects | Influence | Genetic aspects | Research | Methods | Methanol | Proteins | Enzymes | Hydrogen bonds | Index Medicus | Enzymology and Protein Engineering
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3. Full Text Use of ‘small but smart’ libraries to enhance the enantioselectivity of an esterase from Bacillus stearothermophilus towards tetrahydrofuran‐3‐yl acetate
by Nobili, Alberto and Gall, Markus G and Pavlidis, Ioannis V and Thompson, Mark L and Schmidt, Marlen and Bornscheuer, Uwe T
The FEBS journal, ISSN 1742-464X, 07/2013, Volume 280, Issue 13, pp. 3084 - 3093
enantioselectivity | secondary alcohol | tetrahydrofuran‐3‐yl acetate | esterase | directed evolution | tetrahydrofuran-3-yl acetate | Furans - metabolism | Protein Engineering - methods | Stereoisomerism | Molecular Conformation | Bacterial Proteins - chemistry | Substrate Specificity | Acetates - chemistry | Furans - chemistry | Databases, Protein | Recombinant Proteins - metabolism | Catalytic Domain | Computational Biology - methods | Geobacillus stearothermophilus - enzymology | Gene Library | Acetates - metabolism | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Directed Molecular Evolution | Carboxylesterase - metabolism | Hydrolysis | Mutant Proteins - chemistry | Carboxylesterase - genetics | Bacterial Proteins - metabolism | Carboxylesterase - chemistry | Molecular Docking Simulation | Kinetics | Usage | Libraries | Heterocyclic compounds | Analysis | Hydrology | Bacteria | Mutation | Index Medicus
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4. Full Text Efficient Expression of Maltohexaose-Forming α-Amylase from Bacillus stearothermophilus in Brevibacillus choshinensis SP3 and Its Use in Maltose Production
by Li, Zhu and Su, Lingqia and Duan, Xuguo and Wu, Dan and Wu, Jing
BioMed research international, ISSN 2314-6133, 11/2017, Volume 2017, pp. 5479762 - 11
Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Recombinant Proteins - metabolism | Geobacillus stearothermophilus - enzymology | Maltose - metabolism | Bacterial Proteins - genetics | Maltose - analysis | Brevibacillus - metabolism | Geobacillus stearothermophilus - genetics | Recombinant Proteins - genetics | alpha-Amylases - metabolism | Oligosaccharides - metabolism | Brevibacillus - genetics | Fermentation | alpha-Amylases - genetics | Bioreactors | Culture Media | Glucose - metabolism | Bacterial Proteins - metabolism | Cell culture | Biotechnology | Sucrose | Calcium | Laboratories | Proline | Food science | Response surface methodology | pH effects | Syrup | Optimization | Proteins | Engineering | E coli | α-Amylase | Deoxyribonucleic acid--DNA | Enzymes | Starch | Cloning | Corn | Forming | Maltose | Bacteriology | Amylases | Plasmids | Protein expression | Index Medicus
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5. Full Text Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus
by Matsumoto, Yushi and Tosha, Takehiko and Pisliakov, Andrei V and Hino, Tomoya and Sugimoto, Hiroshi and Nagano, Shingo and Sugita, Yuji and Shiro, Yoshitsugu
Nature structural & molecular biology, ISSN 1545-9993, 02/2012, Volume 19, Issue 2, pp. 238 - 245
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Geobacillus stearothermophilus - chemistry | Geobacillus stearothermophilus - enzymology | Mutagenesis, Site-Directed | Oxidoreductases - metabolism | Hydroquinones - chemistry | Mutant Proteins - genetics | Models, Molecular | Crystallography, X-Ray | Mutant Proteins - metabolism | Hydroquinones - metabolism | Oxidoreductases - chemistry | Molecular Dynamics Simulation | Nitrous Oxide - metabolism | Protein Conformation | Nitric Oxide - metabolism | Amino Acid Substitution | Oxidases | Physiological aspects | Genetic aspects | Research | Structure | Nitric oxide | Evolutionary biology | Crystal structure | Index Medicus
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6. Full Text Expression and Characterization of Geobacillus stearothermophilus SR74 Recombinant α-Amylase in Pichia pastoris
by Gandhi, Sivasangkary and Salleh, Abu Bakar and Rahman, Raja Noor Zaliha Raja Abd and Chor Leow, Thean and Oslan, Siti Nurbaya
BioMed research international, ISSN 2314-6133, 5/2015, Volume 2015, pp. 529059 - 529059
Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Gene Expression Regulation, Enzymologic | Geobacillus stearothermophilus - enzymology | Cloning, Molecular | Pichia - genetics | Geobacillus stearothermophilus - genetics | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | alpha-Amylases - biosynthesis | alpha-Amylases - genetics | Index Medicus
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7. Full Text Catalytic properties of maltogenic α-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles
by Straksys, Antanas and Kochane, Tatjana and Budriene, Saulute
Food chemistry, ISSN 0308-8146, 11/2016, Volume 211, pp. 294 - 299
Immobilization | Maltoghenic α-amylase | Covalent binding | Poly(urethane urea) microparticles | Starch hydrolysis | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Nutrition & Dietetics | Food Science & Technology | Science & Technology | Enzymes, Immobilized - metabolism | Microspheres | Geobacillus stearothermophilus - enzymology | Polyurethanes - chemistry | Catalysis | Glycoside Hydrolases - metabolism | Porosity | Enzymes, Immobilized - analysis | Glycoside Hydrolases - analysis | Index Medicus
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8. Full Text Importance of Trp139 in the product specificity of a maltooligosaccharide-forming amylase from Bacillus stearothermophilus STB04
by Xie, Xiaofang and Qiu, Gaoyuan and Zhang, Ziqian and Ban, Xiaofeng and Gu, Zhengbiao and Li, Caiming and Hong, Yan and Cheng, Li and Li, Zhaofeng
Applied microbiology and biotechnology, ISSN 0175-7598, 12/2019, Volume 103, Issue 23, pp. 9433 - 9442
Life Sciences | Biotechnology | Oligosaccharide cleavage pattern | Microbiology | Maltooligosaccharide-forming amylase | Microbial Genetics and Genomics | Product specificity | Stacking interactions | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Science & Technology | Hydrolysis | Geobacillus stearothermophilus - enzymology | Amylases - genetics | Mutagenesis, Site-Directed | Amino Acids - chemistry | Models, Molecular | Substrate Specificity | Geobacillus stearothermophilus - genetics | Oligosaccharides - biosynthesis | Amylases - chemistry | Binding Sites | Amylases | Tyrosine | Acarbose | Alanine | Starch | Stacking | Oligosaccharides | Leucine | Substrates | Mutants | Mutagenesis | Site-directed mutagenesis | Crystal structure | Index Medicus
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9. Full Text Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29
by Bibi, Zainab and Qader, Shah Ali Ul and Aman, Afsheen
Extremophiles : life under extreme conditions, ISSN 1431-0651, 7/2015, Volume 19, Issue 4, pp. 819 - 827
Life Sciences | Biochemistry, general | Biotechnology | Microbial Ecology | Reusability | Microbiology | Xylanase | Calcium alginate | Immobilization | Thermal stability | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Enzymes, Immobilized - chemistry | Geobacillus stearothermophilus - enzymology | Alginates - chemistry | Bacterial Proteins - chemistry | Enzyme Stability | Hexuronic Acids - chemistry | Glucuronic Acid - chemistry | Endo-1,4-beta Xylanases - chemistry | Index Medicus | Space life sciences
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10. Full Text Improving the thermostability of Geobacillus stearothermophilus xylanase XT6 by directed evolution and site-directed mutagenesis
by Zhang, Zhi-Gang and Yi, Zhuo-Lin and Pei, Xiao-Qiong and Wu, Zhong-Liu
Bioresource technology, ISSN 0960-8524, 2010, Volume 101, Issue 23, pp. 9272 - 9278
Thermostability | Protein engineering | Directed evolution | Xylanase | Semi-rational | Agricultural Engineering | Life Sciences & Biomedicine | Technology | Agriculture | Biotechnology & Applied Microbiology | Energy & Fuels | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Adaptation, Physiological | Amino Acid Sequence | Directed Molecular Evolution - methods | Endo-1,4-beta Xylanases - metabolism | DNA Shuffling | Geobacillus stearothermophilus - enzymology | Temperature | Genetic Testing | Gene Library | Protein Structure, Secondary | Endo-1,4-beta Xylanases - genetics | Enzyme Stability | Half-Life | Models, Molecular | Molecular Sequence Data | Mutagenesis, Site-Directed - methods | Geobacillus stearothermophilus - genetics | Endo-1,4-beta Xylanases - chemistry | Point Mutation - genetics | Polymerase Chain Reaction | Amino Acid Substitution - genetics | Enzyme Activation | Kinetics | Enzymes | Proteins | Stearothermophilus | Amino acids | Evolution | Tolerances | Inactivation | Index Medicus
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