PURIFICATION AND PROPERTIES OF CYCLODEXTRINASE OF BACILLUS MACERANS

被引：62

作者：

DEPINTO, JA

CAMPBELL, LL

机构：

[1] Department of Microbiology, University of Illinois, Urbana

来源：

BIOCHEMISTRY | 1968年 / 7卷 / 01期

关键词：

D O I：

10.1021/bi00841a016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new enzyme, cyclodextrinase, from Bacillus macerans was purified 40-fold by means of ammonium sulfate precipitation, DEAE-cellulose, and recycling Sephadex chromatography. Sedimentation velocity experiments showed a major peak at 23 S and a minor peak at 13 S. The enzyme has a pH optimum of 6.26-6.4, and an energy of activation of 27,400 cal/mole over the temperature range 30-40°. The Km for α-dextrin is 2.62 ± 0.27 × 10−3 m, whereas for β-dextrin it is 2.65 ± 0.09 × 10−3m. © 1968, American Chemical Society. All rights reserved.

引用

页码：121 / &

共 11 条

[1] ANOMERIC INVERSIONS BY GLYCOSIDASES [J].