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Purification and characterization of a novel acid phosphatase from the split gill mushroom Schizophyllum commune
Author(s) -
Zhang GuoQing,
Chen QingJun,
Sun Jian,
Wang HeXiang,
Han ChunHua
Publication year - 2013
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201200218
Subject(s) - schizophyllum commune , histidine , amino acid , chemistry , ion chromatography , acid phosphatase , chromatography , mushroom , size exclusion chromatography , peptide sequence , biochemistry , molecular mass , enzyme , ion exchange , organic chemistry , ion , food science , gene
A monomeric acid phosphatase (ACP) with a molecular mass of 72.5 kDa 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 K m of the purified enzyme for ρ‐nitrophenyl phosphate (ρNPP) was 0.248 mM and the V max was 9.093 × 10 −3 μM/min. ACP activity was strongly inhibited by Al 3+ and Fe 3+ , but enhanced by Co 2+ , Mg 2+ , and Ca 2+ at a concentration of 0.5 mM.