Purification and characterization of a novel serine protease from the mushroom Pholiota nameko(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

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• A novel serine protease, with a molecular mass of 19kDa and the N-terminal sequence of ARTPEAPAEV, was isolated from dried fruiting bodies of the mushroom Pholiota nameko. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, Q-Sepharose and SP-Sepharose, and gel filtration on Superdex 75. It was unadsorbed on DEAE-cellulose and Q-Sepharose but adsorbed on SP-Sepharose. It exhibited an optimum temperature at 50℃, an optimum pH at pH 8.8, a Km of 5.64mg/mL and a Vmax of 0.98μmol/min/mL against substrate casein. A number of metal ions inhibited the enzyme including Pb^<2+>, Mn^<2+>, Ca^<2+>, Hg^<2+>, Zn^<2+>, Cu^<2+>, Co^<2+>, Fe^<3+> and Al^<3+>, with the inhibition of the last two cations being the most potent. K^+ and Mg^<2+> slightly enhanced, while Li^+ moderately potentiated the activity of the protease. The protease was strongly inhibited by phenylmethylsulfonyl fluoride (PMSF), suggesting that it is a serine protease.

著者

• Wu Ying-ying

  State Key Laboratory For Agrobiotechnology And Department Of Microbiology China Agricultural Univers

• Zhang Guo-qing

  Key Laboratory Of Urban Agriculture (north) Of Ministry Of Agriculture Beijing University Of Agricul

• Wang He-xiang

  State Key Laboratory For Agrobiotechnology And Department Of Microbiology China Agricultural Univers

• Guan Gui-Ping

  State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural Univer

• Ng Tzi-Bun

  School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong

• Guan Gui-ping

  State Key Laboratory For Agrobiotechnology And Department Of Microbiology China Agricultural Univers

• Ng Tzi-bun

  School Of Biomedical Sciences Faculty Of Medicine The Chinese University Of Hong Kong

関連論文

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