A highly pH-stable phytase from Yersinia kristeensenii: Cloning, expression, and characterization

Enzyme and Microbial Technology

Volumn 42, Issue 6, 2008, Pages 499-505

  Fu, Dawei ^a   Huang, Huoqing ^a   Luo, Huiying ^a   Wang, Yaru ^a   Yang, Peilong ^a   Meng, Kun ^a   Bai, Yingguo ^a   Wu, Ningfeng ^a   Yao, Bin ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Histidine acid phosphatase; pH stable; Phytase; Pichia pastoris; Yersinia kristeensenii

Indexed keywords

AMINO ACIDS; CLONING; GENE ENCODING; PEPTIDES; PH EFFECTS;

HEAT INACTIVATION; HISTIDINE ACID PHOSPHATASE; INCUBATION; PICHIA PASTORIS; YERSINIA KRISTEENSENII;

ENZYME ACTIVITY;

ACID PHOSPHATASE; PHOSPHORUS; PHYTASE; PHYTATE; SIGNAL PEPTIDE;

APPA GENE; ARTICLE; BACTERIAL GENE; DEGLYCOSYLATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STABILITY; EXPRESSION VECTOR; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PICHIA PASTORIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; SOYBEAN; THERMOSTABILITY; YERSINIA; YERSINIA KRISTEENSENII;

GLYCINE MAX; PICHIA PASTORIS; YERSINIA; YERSINIA INTERMEDIA;

EID: 41149142244     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2008.01.014     Document Type: Article

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