書誌事項
- タイトル別名
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- Purification and Properties of Proteinase with Optimum pH 6.0 from Gouda-type Cheese
- ゴーダタイプ チーズチュウ ニ ソンザイスル シテキ pH6.0 ノ プロティ
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説明
The proteinase in Gouda-type cheese, which was ripened for 5 months, was purified by a combination of DEAE-cellulose and Sephadex G-150. The enzyme was purified about 700 fold with a yeild of 5.3%, and showed homogeneity in disc electrophoresis. The enzyme was most active at pH 6.0, and had a temperature optimum at about 30° with a molecular weight of 230, 000. The enzyme was activated by Co2+ and Mn2+, inhibited by ethylenediaminetetraacetic acid and 1, 10-phenathrolin, and strongly affected by phenylmethylsulfonylfluoride and diisopropyl-fluorophosphate. The enzyme could degrade β-and κ-casein, but had very little effect on αs1-casein. Since the mobility of the decomposed products from β-casein by the enzyme were similar to those of the breakdown products found in ripening cheese, the enzyme may play an important role in casein breakdown during ripening.
収録刊行物
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- 日本畜産学会報
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日本畜産学会報 59 (1), 82-92, 1988
公益社団法人 日本畜産学会
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詳細情報 詳細情報について
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- CRID
- 1390282680169213696
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- NII論文ID
- 130000739454
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- NII書誌ID
- AN00195188
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- ISSN
- 18808255
- 00215309
- 1346907X
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- NDL書誌ID
- 3170466
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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
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- 抄録ライセンスフラグ
- 使用不可