PURIFICATION AND CHARACTERIZATION OF THE AMYLOLYTIC ENZYMES OF SACCHAROMYCOPSIS-FIBULIGERA

被引：15

作者：

GASPERIK, J

KOVAC, L

MINARIKOVA, O

机构：

[1] Slovak Academy of Sciences, Institute of Molecular Biology, 842 51 Bratislava

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1991年 / 23卷 / 01期

关键词：

D O I：

10.1016/0020-711X(91)90004-7

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：

1. A complex of extracellular amylolytic enzymes produced by Saccharomycopsis fibuligera KZ, grown on fine fibre (waste product from corn starch production) and corn-steep liquor, has been studied. 2. alpha-Amylases and glucoamylases, as the main representatives of this complex, were separated by hydrophobic chromatography on Spheron 300 LC. 3. Individual isoenzymes of one type were separated on FPLC-Mono Q.4. The relative molecular weight of alpha-amylases is 54,000, glucoamylases 62,000, maximal activity is reached by both enzymes between pH 5.0 and 6.2 at a temperature of 40-50-degrees-C. 5. Glucoamylases have a higher stability of the native structure than alpha-amylases, they retain 55% of their original activity, even after 10 min of incubation at 100-degrees-C.

引用

页码：21 / 25

页数：5

共 18 条

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