Five mutations in N-terminus confer thermostability on mesophilic xylanase

Biochemical and Biophysical Research Communications

Volumn 395, Issue 2, 2010, Pages 200-206

  Zhang, Shan ^a   Zhang, Kai ^b   Chen, Xiuzhen ^a   Chu, Xin ^a   Sun, Fei ^b   Dong, Zhiyang ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Chimera; Mutant; N terminus; Thermostability; Xylanase

Indexed keywords

ENDO 1,4 BETA XYLANASE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; ASPERGILLUS NIGER; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; GENE CLUSTER; GENE MUTATION; GENETIC ANALYSIS; MESOPHILIC BACTERIUM; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; STREPTOMYCES; STREPTOMYCES LIVIDANS; THERMOMONOSPORA; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BETA-GLUCOSIDASE; ENDO-1,4-BETA XYLANASES; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; STREPTOMYCES;

ASPERGILLUS NIGER; STREPTOMYCES; STREPTOMYCES LIVIDANS; THERMOBIFIDA FUSCA;

EID: 77951620702     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.03.159     Document Type: Article

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