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Volumn 160, Issue 8, 2010, Pages 2401-2414
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Erratum: α-Amylase: An ideal representative of thermostable enzymes (Applied Biochemistry and Biotechnology DOI: 10.1007/s12010-009-8735-4);α-Amylase: An ideal representative of thermostable enzymes
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Author keywords
Rigidity; Structural flexibility; Thermostability; Unfolding state; Amylase
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Indexed keywords
RIGIDITY;
STABILITY;
ALPHA AMYLASE;
STRUCTURAL BASIS;
STRUCTURAL FLEXIBILITIES;
THERMOSTABILITY;
THERMOSTABLE ENZYMES;
UNFOLDING STATE;
AMYLASES;
AGLYCONE;
ALANINE;
AMYLASE;
AMYLOPECTIN;
ARGININE;
ASPARTIC ACID;
CALCIUM CHLORIDE;
CALCIUM ION;
CARBOXYLIC ACID;
CHLORIDE ION;
DEOXYRIBONUCLEASE;
DISULFIDE;
GLUTAMIC ACID;
GLYCINE;
GLYCOGEN;
GLYCOSIDE;
HISTIDINE;
HYDROGEN;
NUCLEOPHILE;
OLIGOSACCHARIDE;
PROLINE;
SERINE;
SODIUM ION;
STABILIZING AGENT;
STARCH;
SUGAR;
THREONINE;
TRIOSEPHOSPHATE ISOMERASE;
TYROSINE;
VALINE;
ALPHA HELIX;
AMINO ACID SEQUENCE;
ASPERGILLUS ORYZAE;
BACILLUS AMYLOLIQUEFACIENS;
BACILLUS LICHENIFORMIS;
BACILLUS SUBTILIS;
CARBOHYDRATE METABOLISM;
CATALYSIS;
CHEMICAL MODIFICATION;
CHICKEN;
COST EFFECTIVENESS ANALYSIS;
DIFFERENTIAL SCANNING CALORIMETRY;
DISULFIDE BOND;
DNA SHUFFLING;
ENCAPSULATION;
ENZYME ACTIVITY;
ENZYME INACTIVATION;
ENZYME MODIFICATION;
ENZYME SPECIFICITY;
ESCHERICHIA COLI;
FLUORESCENCE;
GELATINIZATION;
GENE EXPRESSION;
GEOBACILLUS STEAROTHERMOPHILUS;
GLYCOSYLATION;
HYDROGEN BOND;
HYDROPHOBICITY;
INDUSTRIAL PRODUCTION;
INFRARED SPECTROSCOPY;
LIQUEFACTION;
METAL BINDING;
MOLECULAR CLONING;
MOLECULAR WEIGHT;
MUTAGENESIS;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PH;
POLYMERASE CHAIN REACTION;
PROTEIN DEGRADATION;
PROTEIN ENGINEERING;
PROTEIN FOLDING;
PROTEIN FUNCTION;
PROTEIN IMMOBILIZATION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
PSYCHROPHILIC BACTERIUM;
PYROCOCCUS FURIOSUS;
REVIEW;
SACCHARIFICATION;
SACCHAROMYCES CEREVISIAE;
SALIVA;
SEDIMENTATION;
SITE DIRECTED MUTAGENESIS;
TEMPERATURE;
THERMOPHILIC BACTERIUM;
THERMOSTABILITY;
VISCOSITY;
WILD TYPE;
X RAY CRYSTALLOGRAPHY;
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EID: 77949913204
PISSN: 02732289
EISSN: None
Source Type: Journal
DOI: 10.1007/s12010-010-9073-2 Document Type: Erratum |
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Times cited : (145)
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References (131)
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