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- Title
Purification and characterization of a novel acid phosphatase from the split gill mushroom Schizophyllum commune.
- Authors
Zhang, Guo‐Qing; Chen, Qing‐Jun; Sun, Jian; Wang, He‐Xiang; Han, Chun‐Hua
- 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 K m 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 Al3+ and Fe3+, but enhanced by Co2+, Mg2+, and Ca2+ at a concentration of 0.5 mM.
- Subjects
ACID phosphatase; SCHIZOPHYLLUM commune; ION exchange chromatography; AMINO acid sequence; LIQUID chromatography; ENZYME kinetics
- Publication
Journal of Basic Microbiology, 2013, Vol 53, Issue 10, p868
- ISSN
0233-111X
- Publication type
Article
- DOI
10.1002/jobm.201200218