51963
Esterase from Bacillus subtilis
recombinant, expressed in E. coli, ≥0.8 U/mg
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recombinant
expressed in E. coli
form
crystalline, crystals, powder or flakes
specific activity
≥0.8 U/mg
storage temp.
−20°C
Application
Esterase from Bacillus subtilis is used in protein engineering research and is utilized to study the kinetic resolution of acetates of arylaliphatic tertiary alcohols.
Biochem/physiol Actions
An esterase is a hydrolase that splits esters into acids and alcohols.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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)
XieMei Tang et al.
Critical reviews in eukaryotic gene expression, 22(3), 179-187 (2012-11-13)
Tuberculosis remains one of the most prevalent and deadly infectious diseases, largely due to the emergence of multidrug-resistant and extensive drug-resistant Mycobacterium tuberculosis, especially the coinfection with HIV. Mycobacterium Ag85 complex (Ag85A, B, and C), with a carboxylesterase consensus sequence