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Purification and characterization of a novel acid phosphatase from the split gill mushroom Schizophyllum commune

文献类型： 外文期刊

作者： Zhang, Guo-Qing 1 ; Chen, Qing-Jun 1 ; Sun, Jian 2 ; Wang, He-Xiang 2 ; Han, Chun-Hua 4 ;

作者机构： 1.China Agr Univ, Minist Agr, Key Lab Urban Agr North, Beijing 100094, Peoples R China

2.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100094, Peoples R China

3.China Agr Univ, Dept Microbiol, Beijing 100094, Peoples R China

4.Beijing Acad Agr & Forestry Sci, Inst Anim & Husb Med, Beijing 100097, Peoples R China

关键词： Acid phosphatase;Chromatography;Kinetics;N-terminal amino acid sequence;Schizophyllum commune

期刊名称：JOURNAL OF BASIC MICROBIOLOGY （ 影响因子：2.281； 五年影响因子：2.516 ）

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收录情况： SCI

摘要： A monomeric acid phosphatase (ACP) with a molecular mass of 72.5kDa was purified from fresh fruiting bodies of cultured Schizophyllum commune mushroom. The isolation procedure entailed ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. It demonstrated a unique N-terminal amino acid sequence of NAPWAQIDEV, which exhibited 60% amino acid identity to that of S. commune hypothetical histidine ACP based on its genome sequence, but less than 30% amino acid identity to that of other fungal ACPs previously reported. The ACP exhibited an optimum temperature at 50°C, an optimum pH at pH 4.6, and was considerably stable at a pH range of 4.0 to 9.0, and a temperature range of 20-40°C. The Km of the purified enzyme for ρ-nitrophenyl phosphate (ρNPP) was 0.248mM and the Vmax was 9.093×10-3μM/min. ACP activity was strongly inhibited by Al3+ and Fe3+, but enhanced by Co2+, Mg2+, and Ca2+ at a concentration of 0.5mM.

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