Fusion of the OsmC domain from esterase EstO confers thermolability to the cold-active xylanase Xyn8 from Pseudoalteromonas arctica

Extremophiles

Volumn 15, Issue 2, 2011, Pages 311-317

  Elleuche, Skander ^a   Piascheck, Henning ^a   Antranikian, Garabed ^a  

^a HAMBURG UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

Esterase; Gene fusion; OsmC; Pseudoalteromonas arctica; Thermolability; Xylanase

Indexed keywords

BACTERIAL PROTEIN; CARBOXYLESTERASE; ENDO 1,4 BETA XYLANASE; ESCHERICHIA COLI PROTEIN; OSMC PROTEIN, E COLI; RECOMBINANT PROTEIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

ARTICLE; CATALYSIS; CHEMISTRY; COLD; ENZYMOLOGY; GENE EXPRESSION REGULATION; KINETICS; MOLECULAR CLONING; PH; PROTEIN TERTIARY STRUCTURE; PSEUDOALTEROMONAS; TEMPERATURE;

BACTERIAL PROTEINS; CARBOXYLESTERASE; CATALYSIS; CLONING, MOLECULAR; COLD TEMPERATURE; ENDO-1,4-BETA XYLANASES; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN STRUCTURE, TERTIARY; PSEUDOALTEROMONAS; RECOMBINANT PROTEINS; TEMPERATURE; XYLAN ENDO-1,3-BETA-XYLOSIDASE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOALTEROMONAS;

EID: 79952252539     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-011-0361-8     Document Type: Article

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