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J Basic Microbiol. 2013 Oct;53(10):868-75. doi: 10.1002/jobm.201200218. Epub 2013 Jan 15.

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

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1
Key Laboratory of Urban Agriculture (North) of Ministry of Agriculture, Beijing University of Agriculture, Beijing, China.

Abstract

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 Km of the purified enzyme for ρ-nitrophenyl phosphate (ρNPP) was 0.248 mM and the Vmax 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.

KEYWORDS:

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

PMID:
23322529
DOI:
10.1002/jobm.201200218
[Indexed for MEDLINE]
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