DICP OpenIR
Subject Area物理化学
蜗牛酶中水解人参皂甙Rb1的β-D-葡萄糖苷酶的分离纯化及其性质研究
栾宏伟; 齐小辉; 杨凌*; 杨凌
Conference Namethe 2 international Science and Technology Conference of Traditional Chinese Medicine Modernization
Conference Date2005-9-24
2005-09-24
Conference Place中国
Alternative Title蜗牛酶中水解人参皂甙Rb1的β-D-葡萄糖苷酶的分离纯化及其性质研究
Pages382/1
ISSN7-5364-5832-0
Department十八室
Other AbstractAbstract: A β-D-glucosidase from the China white jade snail enzyme had been purified to apparent homogeneity using a combination of anion-exchange, hydrophobic-interaction and gel-permeation chromatography. The enzyme hydrolyzed the 20-C, β-(1→6)-glucoside of ginsenoside Rb1(G-Rb1) to ginsenoside Rd (G-Rd), but did not hydrolyze the other β-D-glucosidic bonds of G-Rb1. This purified glucosidase consisted of two same subunits and had Mr of 230kDa as determined by SDS-PAGE and gel-permeation chromatography. Maximal β-D-glucosidase activity occurred at 70℃ and pH5.6. At pH5.6 and 50℃ the Km for p-nitrophenyl-β-D-glucopyranoside (pNPG) was 0.338mM and it had a Vmax of 0.25mmol nitrophenol/min/mg glucosidase. Theβ-D-glucosidase exhibited low levels of activity against other artificial substrates, compared to its activity against pNPG.
Language中文
Document Type会议论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/111858
Collection中国科学院大连化学物理研究所
Corresponding Author杨凌
Recommended Citation
GB/T 7714
栾宏伟,齐小辉,杨凌*,等. 蜗牛酶中水解人参皂甙Rb1的β-D-葡萄糖苷酶的分离纯化及其性质研究[C],2005:382/1.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[栾宏伟]'s Articles
[齐小辉]'s Articles
[杨凌*]'s Articles
Baidu academic
Similar articles in Baidu academic
[栾宏伟]'s Articles
[齐小辉]'s Articles
[杨凌*]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[栾宏伟]'s Articles
[齐小辉]'s Articles
[杨凌*]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.