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Merck
CN

96667

酯酶 来源于枯草芽孢杆菌

recombinant, expressed in E. coli, ≥10 U/mg

别名:

Carboxylesterase

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关于此项目

化学文摘社编号:
MDL number:
UNSPSC Code:
12352204
EC Number:
232-773-7
NACRES:
NA.54
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产品名称

酯酶 来源于枯草芽孢杆菌, recombinant, expressed in E. coli, ≥10 U/mg

recombinant

expressed in E. coli

form

crystalline
crystals
powder or flakes

specific activity

≥10 U/mg

storage temp.

−20°C

Quality Level

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Application

来自枯草芽孢杆菌的酯酶可用于蛋白质工程研究以及对芳基脂族叔醇乙酸酯的动力学分辨进行研究。产品96667是经重组并大肠杆菌(≥10 U/mg)中表达的。

Biochem/physiol Actions

酯酶可参与酯的立体定向水解和生产。从培养的细菌和真菌中获得的酯酶具有多种工业应用。
酯酶是将酯分解为酸和醇的水解酶。

General description

酯酶属于水解酶超家族。该重组酯酶含有一个C末端组氨酸标签。

Other Notes

1U相当于在 pH 7.5,30°C 下每分钟转化1 μmol 4-硝基苯基-L-乙酸盐的酶量。

Packaging

无底玻璃瓶。内含物在插入的融合锥体内。

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

存储类别

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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High-Resolution Fractionation Processes
Separation Science and Technology, 1, 61-99 (1998)
Birgit Heinze et al.
Protein engineering, design & selection : PEDS, 20(3), 125-131 (2007-02-21)
Enzyme-catalyzed kinetic resolutions of secondary alcohols are a standard procedure today and several lipases and esterases have been described to show high activity and enantioselectivity. In contrast, tertiary alcohols and their esters are accepted only by a few biocatalysts. Only
New citation. Highly Enantioselective Synthesis of Arylaliphatic Tertiary Alcohols using Mutants of an Esterase from Bacillus subtilis
Robert Kourist, Sebastian Bartsch, et al.
Advanced Synthesis & Catalysis, 349, 1393-1398 (2007)
Soil-based gene discovery: a new technology to accelerate and broaden biocatalytic applications
Gray K A, et al.
Advances in Applied Microbiology, 52, 1-28 (2003)
Jessica Lusty Beech et al.
RSC advances, 12(13), 8119-8130 (2022-04-16)
Esterase enzymes catalyze diverse hydrolysis reactions with important biological, commercial, and biotechnological applications. For the improvement of these biocatalysts, there is a need for widely accessible, inexpensive, and adaptable activity screening assays that identify enzymes with particular substrate specificities. Natural

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