Purification and properties of isoflavone-glucosidase.
- Author:
Ming-Jie XIE
1
;
Ming SONG
;
Cui-Xia ZOU
;
Chun-Hua XU
;
Ming-Chun LU
;
Feng-Xie JIN
Author Information
1. College of Life Science, Liaoning Normal University, Dalian 116029, China. xmj1222@sina.com
- Publication Type:Journal Article
- MeSH:
Absidia;
enzymology;
Glucosidases;
isolation & purification;
metabolism;
Hydrogen-Ion Concentration;
Isoflavones;
metabolism;
Temperature
- From:
Chinese Journal of Biotechnology
2006;22(4):635-638
- CountryChina
- Language:Chinese
-
Abstract:
A high activity isoflavone-glucosidase, which hydrolysis glycosides, was obtainde using liquid fermentation from Absidia sp. R strain. The isoflavone-glucosidase was purified 11 folds with yielding rate of 10.9% after ammonium sulfate precipitation and DEAE-Cellocuse (DE-52) ion exchange chromatography. SDS-PAGE results showed that the molecular weight is 53kD. And the optimum temperature, the optimum pH, Km and pI of the enzyme are 50 deegrees C, 5.0, 1.3 x 10(-2) mol/L and 3.2, respectively. The isoflavone-glucosidase is also rather stable under 60 degrees C and in pH range from 5.0 to 7.0. The enzyme can be activated by Co2+ and Ca2+, and be inhibited by Ag+ and Cu2+.
