Purification of an Aspergillus oryzae Metallo-proteinase by Talopeptin-aminohexyl-Sepharose and Its Properties
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概要
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Simple and speedy purification of Aspergillus oryzae metallo-proteinase was performed using Talopeptin-aminohexyl-Sepharose. The properties of the metallo-proteinase were: optimum pH 6.5; pH stability, pH 5-11; optimum temperature, 50°C; and molecular weight 42, 000 (SDS electrophoresis). These results were similar to those of neutral protease I from Aspergillus oryzae reported by Nakadai et al. This metallo-proteinase was compared with others from microbes using the metallo-proteinase inhibitors FMPI, PLT, and Talopeptin. The metallo-proteinase is unique in the point at which FMPI and PLT gave nearly stoichiometrical inhibition.
- 社団法人 日本農芸化学会の論文
著者
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Murao Sawao
Laboratory Of Applied Microbiology College Of Agriculture
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KASAI Naoya
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, University of Osaka Prefecture
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FUKUHARA Ken-ichi
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, University of Osaka Prefecture
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