An alkaline protease inhibitor from Aspergillus oryzae W-1

被引:0
|
作者
Ishihara, M [1 ]
Katayama, H [1 ]
Taira, T [1 ]
Tawata, S [1 ]
Kobamoto, N [1 ]
机构
[1] Univ Ryukyus, Fac Agr, Dept Biosci & Biotechnol, Nishihara, Okinawa 9030213, Japan
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中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
An alkaline protease inhibitor (API) from Aspergillus oryzae W-1 was purified to homogeneity by DEAE-Cellulose and Hvdroxyl apatite column chromategraphies. The molecular mass of the inhibitor was estimated to be 14 KDa by SDS-PAGE and 12.5KDa by gel filtration on Sephadex G-50 column chromatography; the isoelectric point was 4.6. API was extremely heat stable and retained 100% of its original activity even after heating in a boiling water bath for 5 min in the pH range of 4-6. API exhibited an inhibitory activity against the proteolytic activity of alkaline protease from A. oryzae or A. oryzae W-1 but not for subtilisin, subtilisin BPN', papain. ficin. bromelain, trypsin and a-chymotrypsin. It was found that the inhibitor was inactivated by the action of the latter seven enzymes.
引用
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页码:327 / 330
页数:4
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