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

The gene appA, encoding a phytase from Yersinia kristeensenii, was cloned and heterologously expressed in Pichia pastoris. The open reading frame of appA comprised 1326 bp encoding a protein of 441 amino acids including a 24-amino acid signal peptide. The encoded phytase, APPA, was 87% identical to...

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Published inEnzyme and microbial technology Vol. 42; no. 6; pp. 499 - 505
Main Authors Fu, Dawei, Huang, Huoqing, Luo, Huiying, Wang, Yaru, Yang, Peilong, Meng, Kun, Bai, Yingguo, Wu, Ningfeng, Yao, Bin
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Inc 05.05.2008
Elsevier Science
Subjects
Biological and medical sciences
Biotechnology
Fundamental and applied biological sciences. Psychology
Histidine acid phosphatase
pH stable
Phytase
Pichia pastoris
Yersinia
Yersinia kristeensenii
Histidine acid phosphatase
Phytase
pH stable
Pichia pastoris
Yersinia kristeensenii
Ascomycota
4-Phytase
Enzyme
Yersinia
Phosphoric monoester hydrolases
Esterases
Fungi
Characterization
Histidine
pH
Bacteria
Hydrolases
Acid phosphatase
Enterobacteriaceae
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Summary:The gene appA, encoding a phytase from Yersinia kristeensenii, was cloned and heterologously expressed in Pichia pastoris. The open reading frame of appA comprised 1326 bp encoding a protein of 441 amino acids including a 24-amino acid signal peptide. The encoded phytase, APPA, was 87% identical to the phytase from Y. intermedia but was <52% identical to other histidine acid phosphatases. The purified recombinant phytase had an optimal activity at 55 °C and pH 4.5, and it exhibited enzymatic activity between pH 2.0 and 6.5, with a specific activity of 2656 U mg −1 at pH 4.5 and 37 °C. r-APPA retained more than 90% of its initial activity after being incubated under varying pH conditions (pH 1.5–11.0) at 37 °C for 3 h. r-APPA was resistant to heat inactivation, as it retained 46% of its initial activity after incubation at 80 °C for 10 min. r-APPA was effective for the hydrolysis of phytate phosphorus from soybean meal in vitro. Comparison of r-APPA with other well-known phytases suggests that the Y. kristeensenii phytase would be an attractive enzyme for feed industry use.
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ISSN:0141-0229
1879-0909
DOI:10.1016/j.enzmictec.2008.01.014