Structure-based rational design to enhance the solubility and thermostability of a bacterial laccase Lac15

PLoS ONE

Volumn 9, Issue 7, 2014, Pages

  Fang, Zemin ^a,b   Zhou, Peng ^a,b   Chang, Fei ^a,b   Yin, Qiang ^a,b   Fang, Wei ^a,b   Yuan, Jing ^a,b   Zhang, Xuecheng ^a,b   Xiao, Yazhong ^a,b  

^a ANHUI UNIVERSITY   (China)

^b Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis   (China)

Author keywords

[No Author keywords available]

Indexed keywords

LACCASE; BACTERIAL PROTEIN; CHROMOGENIC SUBSTRATE; HAIR DYE; HYBRID PROTEIN;

ALKALINITY; ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; HAIR COLOR; HIGH TEMPERATURE; LAC15 GENE; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN EXPRESSION; SOLUBILITY; THERMOSTABILITY; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME SPECIFICITY; ESCHERICHIA COLI; HEAT; METABOLISM; PH; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

BACTERIAL PROTEINS; CATALYSIS; CHROMOGENIC COMPOUNDS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HAIR DYES; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; LACCASE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84904569890     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0102423     Document Type: Article

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