Inducement, Purification and Characterization of?-mannanase from Armillariella tabescens EJLY2098
- VernacularTitle:Armillariella tabescens EJLY2098?-甘露聚糖酶的诱导、纯化及酶学性质分析
- Author:
Dong-Sheng YAO
;
Xiao-Kui HUANG
;
Da-Ling LIU
;
Chun-Fang XIE
;
Rong HU
;
- Publication Type:Journal Article
- Keywords:
Konjac?-mannanase Purification Armillariella tabescens EJLY2098
- From:
China Biotechnology
2006;0(07):-
- CountryChina
- Language:Chinese
-
Abstract:
Armillariella tabescens EJLY2098 was capable of secreting p-mannanase by konjac inducement. A 34 orthogonal design was applied to determine the optimum medium of inducing mannanase by Armillariella tabescens EJLY2098. The results suggested that Armillariella tabescens EJLY2098 secreted the high-activity enzyme in the optimum medium, which was composed of 2% konjac, 1% peptone, 25% potato juice,0.3% KH2PO4,15% MgSO4?7H2O, 0.01% VitB1. Purified by DEAE-anion exchange chromatography, two eluting peaks (P1 and P2) with the p-mannanase activity were obtained, and one of them (named?-mannanase P2) was a single band by the SDS-PAGE, and the molecular weight of?-mannanase P2 was 78. 9kDa. The isoelectric point of?-mannanase P2 was estimated to be 4.0-4. 1. The optimum activity for the enzyme was found at 60℃and pH4. 0 - 6. 0, and the enzyme was stable between pH4. 5 - 6. 0. The activity of?-mannanase P2 were enhanced by Na+ and Ba2+ . This?-mannanase can be used in feed industy. a new fungi secreting?-mannanase was obtained, providing an important base for cloning mannanase gene and constructing recombin microbe expressing?-mannanase .
