Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: Implications for a comprehensive thermostabilization strategy

Biotechnology and Bioengineering

Volumn 108, Issue 8, 2011, Pages 1841-1851

  Chen, Shuo ^a,b,c   Ye, Fengchun ^a   Chen, Yang ^a   Chen, Yu ^a   Zhao, Hongxin ^a   Yatsunami, Rie ^b   Nakamura, Satoshi ^b   Arisaka, Fumio ^b   Xing, Xin Hui ^a  

^a TSINGHUA UNIVERSITY   (China)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

Dimerization; Heparinase; Inactivation; Kinetic modeling; Stabilization; Unfolding

Indexed keywords

BIOCHEMICAL ANALYSIS; BIOCHEMICAL STUDIES; CONTAMINATION DETECTION; E. COLI; ENZYMATIC DEGRADATION; ENZYME CONCENTRATIONS; EXPERIMENTAL DATA; HEPARINASE; HIGH YIELD; INACTIVATION; INACTIVATION MECHANISMS; INACTIVATION MODELS; INTERMOLECULAR DISULFIDE BOND; KINETIC MODELING; LOW-MOLECULAR WEIGHT HEPARINS; MALTOSE BINDING PROTEINS; OPTIMUM TEMPERATURE; PHARMACEUTICAL INDUSTRY; THERMAL INACTIVATION; THERMAL STABILIZATION; THERMOSTABILIZATION; TWEEN 80; UNFOLDING;

BIODEGRADATION; COVALENT BONDS; DEGRADATION; DIMERIZATION; ENZYMES; ESCHERICHIA COLI; KINETIC THEORY; KINETICS; POLLUTION DETECTION; POLYSACCHARIDES; STABILIZATION; STRUCTURAL ANALYSIS;

IGNEOUS ROCKS;

CALCIUM ION; HEPARIN LYASE; HEPARIN LYASE 1; MALTOSE BINDING PROTEIN; POLYSORBATE 80; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL ANALYSIS; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; ESCHERICHIA COLI; KINETICS; PROTEIN UNFOLDING; TEMPERATURE; THERMOSTABILITY;

CALCIUM; DITHIOTHREITOL; ENZYME ACTIVATORS; ENZYME STABILITY; ESCHERICHIA COLI; HEPARIN LYASE; KINETICS; MALTOSE-BINDING PROTEINS; MUTAGENESIS, SITE-DIRECTED; POLYSORBATES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; TEMPERATURE;

EID: 79959199497     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.23144     Document Type: Article

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