書誌事項
- タイトル別名
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- Purification and Characteristics of Milk Clotting Protease from Aspergillus ustus.
- Aspergillus ustus ギョウニュウセイ プロテアーゼ ノ セイセ
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抄録
A strain of mold having milk clotting protease was isolated from soil, and identified as Aspergillus ustus. The crude enzyme from wheat bran culture was purified by salting-out and several column chromatographic methods. In the final stage, the enzyme was refined to a unique protein of which milk clotting activity (MCA) was 18.7 fold of the crude enzyme. The molecular weight was estimated to be 86 kDa. MCA increased with a decrease of pH within the pH range 5.0 to 6.75 but proteolytic activity (PA) was optimum at pH 6.0, and both activities were stable in pH 6.3-6.0. Optimum temperature was 63°C for MCA and 50°C for PA. Inactivation by heating was observed at 55°C in both MCA and PA. Ca2+ was much effective on MCA, but not on PA. Km value of PA to casein was 0.27%. Some metal ions affected both activities, and inhibition of NEM and SDS were considerable. Decomposition of αs1-casein was lower, and that of β-casein was higher by the A. ustus enzyme than by chymosin, but no considerable difference in their activities was observed toward k-casein.
収録刊行物
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- 日本食品工業学会誌
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日本食品工業学会誌 40 (4), 256-261, 1993
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
- 1390282681382662272
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- NII論文ID
- 130003968104
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- NII書誌ID
- AN00192587
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- COI
- 1:CAS:528:DyaK3sXkt1egs7Y%3D
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- NDL書誌ID
- 3825720
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- ISSN
- 00290394
- http://id.crossref.org/issn/00290394
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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