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96667

Sigma-Aldrich

Esterase from Bacillus subtilis

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

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Synonym(s):
Carboxylesterase
CAS Number:
9016-18-6
Enzyme Commission number:
3.1.1.1 (BRENDA, IUBMB)
EC Number:
232-773-7
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

100

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
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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High-Resolution Fractionation Processes
Separation Science and Technology, 1, 61-99 (1998)
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
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
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