Deletion and site-directed mutagenesis of laccase from Shigella dysenteriae results in enhanced enzymatic activity and thermostability

Enzyme and Microbial Technology

Volumn 44, Issue 5, 2009, Pages 274-280

  Shao, Xiaohu ^a   Gao, Yinghui ^a   Jiang, Mengtian ^a   Li, Lin ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Characterization; Enhancement; Enzyme active; Laccase; Mutagenesis; Shigella dysenteriae

Indexed keywords

E. COLI; ENHANCEMENT; ENZYMATIC ACTIVITIES; FUSION PROTEINS; HIGH YIELDS; HIGHER TEMPERATURES; LACCASE; LACCASE GENES; LACCASES; PH OPTIMUM; SHIGELLA DYSENTERIAE; SITE-DIRECTED MUTAGENESIS; THIOGLYCOLIC ACIDS; WILD TYPES;

DIFFUSERS (OPTICAL); ENZYMES; ESCHERICHIA COLI; METAL IONS; METAL REFINING; MUTAGENESIS; PURIFICATION;

ENZYME ACTIVITY;

2,2' AZINOBIS(3 ETHYLBENZOTHIAZOLINE 6 SULFONIC ACID); COPPER; EDETIC ACID; LACCASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GENE DELETION; GENE EXPRESSION; GENE SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; SHIGELLA DYSENTERIAE; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

ESCHERICHIA COLI; SHIGELLA DYSENTERIAE;

EID: 61349134731     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2008.12.013     Document Type: Article

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