Abstract:
:Beta-D-Xylosidase (EC 3.2.1.37) has been purified from ginsenoside Ra-metabolizing Bifidobacterium breve K-110, which was isolated from human intestinal microflora. beta-D-Xylosidase was purified to apparent homogeneity by a combination of ammonium sulfate precipitation, QAE-cellulose, butyl-toyopearl, hydroxyapatit and Q-Sepharose column chromatographies with the final specific activity of 51.8 micromol/min/mg. Molecular weight of beta-D-xylosidase is 49 kDa by SDS-PAGE and gel filtration, which consisted of a single subunit. beta-D-Xylosidase showed optimal activity at pH 5.0 and 37 degrees C. The purified enzyme was potently inhibited by PCMS. beta-D-Xylosidase acted to the greatest extent on p-nitrophenyl-beta-D-xylopyranoside, followed by ginsenoside Ra1 and ginsenoside Ra2. This enzyme hydrolyzed xylan to xylose, but did not act on p-nitrophenyl-beta-glucopyranoside, p-nitrophenyl-beta-galactopyranoside or p-nitrophenyl-beta-D-fucopyranoside. These findings suggest that this is the first reported purification of ginsenoside-hydrolyzing beta-D-xylosidase from an anaerobic Bifidobacterium sp.
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Shin HY,Lee JH,Lee JY,Han YO,Han MJ,Kim DHdoi
10.1248/bpb.26.1170subject
Has Abstractpub_date
2003-08-01 00:00:00pages
1170-3issue
8eissn
0918-6158issn
1347-5215journal_volume
26pub_type
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更新日期:2014-01-01 00:00:00
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pub_type: 杂志文章
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更新日期:1999-04-01 00:00:00
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更新日期:2004-07-01 00:00:00
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pub_type: 杂志文章
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更新日期:2010-01-01 00:00:00
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pub_type: 杂志文章
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更新日期:2003-05-01 00:00:00
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pub_type: 杂志文章
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更新日期:2013-01-01 00:00:00
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journal_title:Biological & pharmaceutical bulletin
pub_type: 杂志文章
doi:10.1248/bpb.22.227
更新日期:1999-02-01 00:00:00
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更新日期:2002-04-01 00:00:00
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更新日期:2001-03-01 00:00:00
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更新日期:2004-02-01 00:00:00
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更新日期:2010-01-01 00:00:00
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更新日期:1997-05-01 00:00:00
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更新日期:2004-11-01 00:00:00
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