96667
Esterase from Bacillus subtilis
recombinant, expressed in E. coli, ≥10 U/mg
Sinonimo/i:
Carboxylesterase
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About This Item
Prodotti consigliati
Ricombinante
expressed in E. coli
Forma fisica
crystalline
crystals
powder or flakes
Attività specifica
≥10 U/mg
Temperatura di conservazione
−20°C
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Descrizione generale
Esterase belongs to the hydrolase superfamily of enzymes.This recombinant esterase contains a C-terminal histidine tag.
Applicazioni
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).
Azioni biochim/fisiol
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.
Confezionamento
Bottomless glass bottle. Contents are inside inserted fused cone.
Definizione di unità
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.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Resp. Sens. 1
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
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I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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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