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

文献类型: 外文期刊

第一作者: Zhang, Guo-Qing

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

作者机构:

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.

分类号: R37

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