The N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates

Acta Biochimica et Biophysica Sinica

Volumn 40, Issue 11, 2008, Pages 949-954

  Ding, Ming ^a   Teng, Yigang ^a   Yin, Qiuyu ^a   Zhao, Jie ^b   Zhao, Fukun ^a,b  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b ZHEJIANG SCI TECH UNIVERSITY   (China)

Author keywords

Ampullaria crossean; Cellulose binding domain; CMCase; EGXA; Endo 1,4 glucanase; Endo 1,4 xylanase; PNPCase

Indexed keywords

CELLULOSE; PRIMER DNA; RECOMBINANT PROTEIN; XYLAN 1,4 BETA XYLOSIDASE;

ANIMAL; ARTICLE; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; ENZYME STABILITY; METABOLISM; MOLLUSC; NUCLEOTIDE SEQUENCE; TEMPERATURE;

ANIMALS; BASE SEQUENCE; BINDING SITES; CELLULOSE; DNA PRIMERS; ENZYME STABILITY; MOLLUSCA; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TEMPERATURE; XYLOSIDASES;

AMPULLARIA; AMPULLARIA CROSSEAN; HEXAPODA; MOLLUSCA;

EID: 57349150248     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2008.00481.x     Document Type: Article

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