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Merck

96667

Sigma-Aldrich

Esterase aus Bacillus subtilis

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

Synonym(e):

Carboxylesterase

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About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in E. coli

Qualitätsniveau

Form

crystalline
crystals
powder or flakes

Spezifische Aktivität

≥10 U/mg

Lagertemp.

−20°C

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Allgemeine Beschreibung

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

Anwendung

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. Wirkung

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.

Verpackung

Bottomless glass bottle. Contents are inside inserted fused cone.

Einheitendefinition

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.

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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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)
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)
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

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