Corticium rolfsiiの酸性proteinase

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URI http://shark.lib.kagawa-u.ac.jp/kuir/metadata/2581
Title
Corticium rolfsiiの酸性proteinase
Title Alternative
Acid proteinase from Corticium rolfsii
File
Description

On the basis of screening Corticium species, acid proteinase was found to be produced by all 13 strains used. Corticium rolfsii IFO 4878 was selected for the enzymatic study and cultured in a medium containing defatted soybean powder. Acid proteinase was partially purified about 68-fold from the culture fluid by a combination of various column chromatography. The isoelectric point lied at pH 4.33 and the molecular weight was estimated to be 27,500. The enzymatic activity was found to be maximum at pH 2.5 toward milk casein and at 2.0 toward hemoglobin-HCl. The enzyme was stable between pH 1.0 and 5.0. At pH 1.0, the enzyme lost less than 10% of its activity during a 72-hr period at 4℃. The enzymatic activity was inhibited by pepstatin, 1,2-epoxy-3-(p-nitrophenoxy) propane, CN-and Hg2+, but stimulated by Mn2+. The enzyme had an optimal pH for milk-clotting activity between 5.3 and 5.5. The partial purified acid proteinase was demonstrated by its ability to hydrolyze various native proteins.

Corticium属のスクリーニングの結果, 用いた13菌株のすべてが酸性プロテアーゼを生産した. この中からCorticium rolfsii IFO 4878を選択し, 脱脂大豆粉末を培養基として培養した. 培養液より酵素を約68倍に部分精製した. 酵素の等電点はpH4.33, 分子量は約27,500であった. 酵素の作用至適pHはミルクカイゼンが基質の場合は約2.5, ヘモグロビン-HClの場合は約2.0であった. 酵素はpH 1.0から5.0において安定であり, 微生物起源のacid proteinaseでは最も耐酸性に属する. 酵素病性はペプスタチン, 1,2-epoxy-3-(p-nitrophenoxy)-propane, CN-, Hg2+によって阻害されたが, Mn2+によって賦活された. ミルク凝固活性の至適pHは5.3から5.5にあり, 天然蛋白質に対して広い基質特異性を示した.

Author
著者 三好 敏夫
著者(ヨミ) ミヨシ トシオ
著者(別表記) Miyoshi Toshio
著者 上原 哲
著者(ヨミ) ウエハラ サトシ
著者(別表記) Uehara Satoshi
著者 梶 明
著者(ヨミ) カジ アキラ
著者(別表記) Kaji Akira
著者 佐藤 優行
著者(ヨミ) サトウ マサユキ
著者(別表記) Sato Masayuki
Publication Title
香川大学農学部学術報告
Volume
33
Issue
1
Start Page
23
End Page
31
Publisher
香川大学農学部
Published Date
198110
ISSN
0368-5128
NCID
AN00038339
Resource Type
Departmental Bulletin Paper
Language
jpn
Text Version
publisher
Set
香川大学
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