Esterase from Bacillus subtilis

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

CAS Number:
Enzyme Commission number:
EC Number:

Quality Level


expressed in E. coli


powder or flakes

specific activity

≥10 U/mg

storage temp.


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General description

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


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

Esterase participates in the stereospecific hydrolysis and production of esters. Esterases, that are obtained from cultured bacteria and fungi has several industrial applications.


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.


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

High-Resolution Fractionation Processes
Separation Science and Technology, 1, 61-99 (1998)
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)
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)
Marie C Fortin et al.
Drug metabolism and disposition: the biological fate of chemicals, 41(2), 326-331 (2012-12-12)
Studies on therapeutic drug disposition in humans have shown significant alterations as the result of pregnancy. However, it is not known whether pesticide metabolic capacity changes throughout pregnancy, which could affect exposure of the developing brain. We sought to determine...

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