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Merck

96667

Sigma-Aldrich

Esterase from Bacillus subtilis

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

Sinónimos:

Carboxylesterase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

form

crystalline
crystals
powder or flakes

specific activity

≥10 U/mg

storage temp.

−20°C

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General description

Esterase belongs to the hydrolase superfamily of enzymes.This recombinant esterase contains a C-terminal histidine tag.

Application

Esterase, from Bacillus subtilis, may be used in protein engineering research as well as to study the kinetic resolution of acetates of arylaliphatic tertiary alcohols. Product 96667 is recombinant and expressed in E. Coli (≥10 U/mg).

Biochem/physiol Actions

An esterase is a hydrolase that splits esters into acids and alcohols.
Esterase participates in the stereospecific hydrolysis and production of esters. Esterases, that are obtained from cultured bacteria and fungi has several industrial applications.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

1 U corresponds to the amount of enzyme which converts 1 μmol 4-nitrophenyl-L-acetate per minute at pH 7.5 and 30°C.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
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)
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)

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