The improvement of stability, activity, and substrate promiscuity of glycerol dehydrogenase substituted by divalent metal ions

Biotechnology and Bioprocess Engineering

Volumn 18, Issue 4, 2013, Pages 796-800

  Wang, Shizhen ^a   Wang, Jing ^a   Zhou, Xiaofen ^a   Guo, Yingxia ^a   Fang, Baishan ^a  

^a XIAMEN UNIVERSITY   (China)

Author keywords

glycerol dehydrogenase; kinetics; metal ion substitution; substrate promiscuity thermodynamics

Indexed keywords

ENZYME INACTIVATION; GLYCEROL DEHYDROGENASE; INACTIVATION MODELS; KLEBSIELLA PNEUMONIA; METAL ION SUBSTITUTION; THERMAL INACTIVATION; THERMO DYNAMIC ANALYSIS; THERMODYNAMIC PARAMETER;

BACTERIA; ENZYME KINETICS; GLYCEROL; KETONES; MANGANESE; METAL IONS; THERMOANALYSIS; THERMODYNAMICS;

SUBSTRATES;

3 CHLOROACETYLPYRIDINE; 4 CHLOROACETOACETATE; 4 CHLOROACETOPHENONE; ACETOACETIC ACID DERIVATIVE; ACETOPHENONE; ACETOPHENONE DERIVATIVE; GLYCEROL DEHYDROGENASE; MAGNESIUM ION; MANGANESE; METAL ION; PYRIDINE DERIVATIVE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENTHALPY; ENTROPY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INACTIVATION; ENZYME METABOLISM; ENZYME MODIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; KLEBSIELLA PNEUMONIAE; NONHUMAN; PROTEIN FOLDING; THERMODYNAMICS;

EID: 84882643441     PISSN: 12268372     EISSN: 19763816     Source Type: Journal    
DOI: 10.1007/s12257-013-0125-7     Document Type: Article

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