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安全信息

X3504

Sigma-Aldrich

β-Xylosidase, thermostable

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

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About This Item

CAS号:
UNSPSC代码:
12352204

重组

expressed in E. coli

质量水平

方案

≥90% (SDS-PAGE)

表单

liquid

比活

≥35 units/mg protein

分子量

81 kDa

浓度

≥20 mg protein/mL (UV)

运输

wet ice

储存温度

2-8°C

生化/生理作用

Releases reducing sugars from birchwood xylan ( X0502), also catalyzes the hydrolysis of 4-methylumbelliferyl-β-D-cellobioside and 4-methylumbelliferyl-β-D-glucopyranoside. This enzyme does not possess endo-xylanase, arabinoxylanase or β-glucanase activities.
β-Xylosidase undergoes post-translation glycosylation which has been shown to be critical for its proper activity and stability. Deglycosylation altered the the optimum temperature and pH for activity and decreased its thermostability.

单位定义

One xylosidase unit will produce 1 μmole of o-nitrophenol per minute at 70 °C from
a 1mM solution of o-nitrophenyl-β-xyloside in 50 mM sodium acetate at pH 5.8.

外形

Supplied as a solution in 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, and 25% glycerol.

储存分类代码

10 - Combustible liquids

WGK

WGK 2

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Galina Mai-Gisondi et al.
Methods in molecular biology (Clifton, N.J.), 1588, 45-57 (2017-04-19)
Colorimetric detection of reaction products is typically preferred for initial surveys of acetyl xylan esterase (AcXE) activity. This chapter will describe common colorimetric methods, and variations thereof, for measuring AcXE activities on commercial, synthesized, and natural substrates. Whereas assays using
Alexandre Favarin Somera et al.
Journal of microbiology (Seoul, Korea), 47(3), 270-276 (2009-06-27)
Aspergillus versicolor grown on xylan or xylose produces two beta-xylosidases with differences in biochemical properties and degree of glycosylation. We investigated the alterations in the biochemical properties of these beta-xylosidases after deglycosylation with Endo-H or PNGase F. After deglycosylation, both
M Nepi et al.
Annals of botany, 108(3), 521-527 (2011-08-05)
Nectar is a very complex mixture of substances. Some components (sugars and amino acids) are considered primary alimentary rewards for animals and have been investigated and characterized in numerous species for many years. In contrast, nectar proteins have been the
Sriwan Wongwisansri et al.
Bioresource technology, 132, 410-413 (2012-12-26)
A gene coding for thermotolerant β-xylosidase from Aspergillus sp. BCC125 was characterized. The recombinant enzyme was expressed in methylotrophic yeast Pichia pastoris KM71 and especially high yield of secreted enzyme was obtained. β-xylosidase possessed high enzyme efficiency (Kcat/Km=198.8mM(-1)s(-1)) toward pNP-β-D-xylopyranoside
Yang-Jin Hyun et al.
Journal of microbiology and biotechnology, 22(4), 535-540 (2012-04-27)
beta-D-Xylosidase (E.C. 3.2.1.37) from Bifidobacterium breve K-110, which hydrolyzes ginsenoside Ra1 to ginsenoside Rb2, was cloned and expressed in Escherichia coli. The (His6)-tagged recombinant enzyme, designated as XlyBK- 110, was efficiently purified using Ni²⁺-affinity chromatography (109.9-fold, 84% yield). The molecular

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