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 in | Enzyme and microbial technology Vol. 42; no. 6; pp. 499 - 505 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Amsterdam
Elsevier Inc
05.05.2008
Elsevier Science |
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| Abstract | 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. |
|---|---|
| AbstractList | 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-AP with other well-known phytases 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. |
| Author | Luo, Huiying Fu, Dawei Wu, Ningfeng Yang, Peilong Yao, Bin Huang, Huoqing Meng, Kun Bai, Yingguo Wang, Yaru |
| Author_xml | – sequence: 1 givenname: Dawei surname: Fu fullname: Fu, Dawei organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 2 givenname: Huoqing surname: Huang fullname: Huang, Huoqing organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 3 givenname: Huiying surname: Luo fullname: Luo, Huiying organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 4 givenname: Yaru surname: Wang fullname: Wang, Yaru organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 5 givenname: Peilong surname: Yang fullname: Yang, Peilong organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 6 givenname: Kun surname: Meng fullname: Meng, Kun organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 7 givenname: Yingguo surname: Bai fullname: Bai, Yingguo organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 8 givenname: Ningfeng surname: Wu fullname: Wu, Ningfeng organization: Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China – sequence: 9 givenname: Bin surname: Yao fullname: Yao, Bin email: yaobin@caas-bio.net.cn organization: Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China |
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| Cites_doi | 10.1080/17450390009381958 10.1080/713609297 10.2527/1993.71123368x 10.1016/S0065-2164(08)70375-7 10.1016/j.bbrc.2006.09.118 10.1128/AEM.70.5.3041-3046.2004 10.1016/0003-2697(76)90527-3 10.1139/cjm-46-1-59 10.1016/j.anifeedsci.2006.03.016 10.1128/AEM.64.11.4446-4451.1998 10.1007/s00253-005-0005-y 10.1016/0888-7543(95)80010-J 10.1016/S0021-9258(18)52245-6 10.1016/0271-5317(95)00040-P 10.1099/00221287-143-1-245 10.2527/1992.7041159x 10.1021/jf00038a034 10.2527/1993.71123359x 10.1079/BJN19900052 10.1128/AEM.65.5.1915-1918.1999 10.1042/bj0370256 10.1016/S0065-2628(08)60110-X 10.1128/AEM.65.2.367-373.1999 10.1038/nsb0397-185 10.1016/0005-2744(72)90340-3 |
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| Keywords | 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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| Snippet | The gene
appA, encoding a phytase from
Yersinia kristeensenii, was cloned and heterologously expressed in
Pichia pastoris. The open reading frame of
appA... The gene appA, encoding a phytase from Yersinia kristeensenii, was cloned and heterologously expressed in Pichia pastoris. The open reading frame of appA... |
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| SubjectTerms | Biological and medical sciences Biotechnology Fundamental and applied biological sciences. Psychology Histidine acid phosphatase pH stable Phytase Pichia pastoris Yersinia Yersinia kristeensenii |
| Title | A highly pH-stable phytase from Yersinia kristeensenii: Cloning, expression, and characterization |
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