書誌事項
- タイトル別名
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- Purification and Some Properties of an Alkaline Protease Inhibitor-Inactivating-Enzyme from Aspergillus oryzae W-1
- Aspergillus oryzae W 1 ノ アルカリプロテアーゼインヒビター シッカツカ コウソ ノ セイセイ ト セイシツ
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An alkaline protease inhibitor-inactivating enzyme (AIE) of Aspergillus oryzae W-1 was purified to homogeneity by the combination of various column chromatographies. The molecular mass of the enzyme was estimated to be 42 kDa by SDS-PAGE; the isoelectric point was 4.7. AIE was optimally active at around 55°C and pH6. The enzyme was stable up to 40°C and in the pH range of 6-10. AIE was inactivated by HgCl2 or p-chloromercuribenzoate (p-CMB) but not by trypsin inhibitor, leupeptin, and phenylmethylsulfonylfluoride (PMSF). It was also inactivated by chelating agents, like ethylenediaminetetraacetate (EDTA) and o-phenanthroline. The enzyme treated with HgCl2, however, was reactivated by the addition of 2-mercaptoethanol (2-ME). On the other hand, EDTA-inactivated AIE was reactivated in the presence of 2-ME and CaCl2. When the protease-inhibitor complex was incubated with AIE at 37°C and pH5, the activation of AP was detected. From these results, it was supposed that AIE is responsible for the activation of alkaline protease (AP) in the cells of mold.
収録刊行物
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- 日本食品科学工学会誌
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日本食品科学工学会誌 50 (12), 578-581, 2003
公益社団法人 日本食品科学工学会
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詳細情報 詳細情報について
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- CRID
- 1390001206410028416
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- NII論文ID
- 10011871072
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- NII書誌ID
- AN10467499
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- ISSN
- 18816681
- 1341027X
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- NDL書誌ID
- 6800830
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可
