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- IGOSHI Keiji
- Faculty of Agriculture, Kyushu Tokai University
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- KAMINOGAWA Shuichi
- Faculty of Agriculture, The University of Tokyo
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- YAMAUCHI Kunio
- Faculty of Agriculture, The University of Tokyo
Bibliographic Information
- Other Title
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- ゴーダタイプチーズ中に存在する至適pH6.0のプロティナーゼの精製と性質
- 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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Description
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.
Journal
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- Nihon Chikusan Gakkaiho
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Nihon Chikusan Gakkaiho 59 (1), 82-92, 1988
Japanese Society of Animal Science
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Keywords
Details 詳細情報について
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- CRID
- 1390282680169213696
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- NII Article ID
- 130000739454
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- NII Book ID
- AN00195188
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- ISSN
- 18808255
- 00215309
- 1346907X
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- NDL BIB ID
- 3170466
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed