Introduction of glycine and proline residues onto protein surface increases the thermostability of endoglucanase CelA from Clostridium thermocellum

Bioresource Technology

Volumn 102, Issue 3, 2011, Pages 3636-3638

  Yi, Zhuo Lin ^a,b   Pei, Xiao Qiong ^a   Wu, Zhong Liu ^a  

^a CHENGDU INSTITUTE OF BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

CelA; Endoglucanase; Rational design; Saturation mutagenesis; Thermostability

Indexed keywords

CELA; ENDOGLUCANASES; RATIONAL DESIGN; SATURATION MUTAGENESIS; THERMOSTABILITY;

AMINO ACIDS; CLOSTRIDIUM; DESIGN;

MUTAGENESIS;

GLUCAN SYNTHASE; GLYCINE; PROLINE;

AMINO ACID; BACTERIUM; ENZYME ACTIVITY; MUTATION; PROTEIN; SATURATION; TEMPERATURE EFFECT;

ARTICLE; CLOSTRIDIUM THERMOCELLUM; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STRUCTURE; MUTATION; NONHUMAN; PRIORITY JOURNAL; THERMOSTABILITY; WILD TYPE;

CELLULASE; CLOSTRIDIUM THERMOCELLUM; ENZYME ACTIVATION; ENZYME STABILITY; GLYCINE; MUTAGENESIS, SITE-DIRECTED; PROLINE; PROTEIN ENGINEERING; TEMPERATURE;

CLOSTRIDIUM THERMOCELLUM;

EID: 78650826462     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.11.043     Document Type: Article

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