N-Terminal fusion of a hyperthermophilic chitin-binding domain to xylose isomerase from Thermotoga neapolitana enhances kinetics and thermostability of both free and immobilized enzymes

Biotechnology Progress

Volumn 26, Issue 4, 2010, Pages 993-1000

  Harris, James M ^a   Epting, Kevin L ^a   Kelly, Robert M ^a  

^a North Carolina State University   (United States)

Author keywords

Chitin binding domain; Hyperthermophile; Thermotoga neapolitana; Xylose isomerase

Indexed keywords

ACTIVE SITE STRUCTURE; BI-PHASIC; CHITIN BEADS; CHITIN-BINDING DOMAINS; CHITINASES; D-XYLOSE; FUSION PROTEINS; HYPERTHERMOPHILE; HYPERTHERMOPHILIC; IMMOBILIZED ENZYME; INACTIVATION MODELS; N-TERMINALS; PYROCOCCUS FURIOSUS; SUBSTRATE-BINDING; SUBUNIT INTERACTIONS; THERMOTOGANEAPOLITANA; TURNOVER NUMBER; TURNOVER RATE; WILD TYPES; WILD-TYPE ENZYMES; XYLOSE ISOMERASE;

BINDING ENERGY; CATALYSTS; CHITIN; FRUCTOSE; GLUCOSE; XYLOSE;

ENZYMES;

CHITIN; IMMOBILIZED ENZYME; ISOMERASE; RECOMBINANT PROTEIN; XYLOSE ISOMERASE;

ARTICLE; ENZYME STABILITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; THERMOTOGA NEAPOLITANA;

ALDOSE-KETOSE ISOMERASES; CHITIN; ENZYME STABILITY; ENZYMES, IMMOBILIZED; KINETICS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THERMOTOGA NEAPOLITANA;

PYROCOCCUS FURIOSUS; THERMOTOGA NEAPOLITANA;

EID: 77956972987     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.416     Document Type: Article

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