NDLI: Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica

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Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Subinya, Mireia Steudle, Anne K. Nestl, Bettina M. Stubenrauch, Cosima
Description	Author Affiliation: Steudle AK ( Chemistry Department, Durham University, South Road, DH1 3LE Durham (UK).)
Abstract	Selective enzyme-catalysed biotransformations offer great potential in organic chemistry. However, special requirements are needed to achieve optimum enzyme activity and stability. A bicontinuous microemulsion is proposed as reaction medium because of its large connected interface between oil and water domains at which a lipase can adsorb and convert substrates in the oil phase of the microemulsion. Herein, a microemulsion consisting of buffer–n-octane–nonionic surfactant $C_{i}E_{j}$ was used to investigate the key factors that determine hydrolyses of p-nitrophenyl esters catalysed by the lipase B from Candida antarctica (CalB). The highest CalB activity was found around 44 °C in the absence of NaCl and substrates with larger alkyl chains were better hydrolysed than their short-chained homologues. The CalB activity was determined using two different co-surfactants, namely the phospholipid 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and the sugar surfactant decyl β-D-glucopyranoside $(β-C_{10}G_{1}).$ The results show the CalB activity as linear function of both enzyme and substrate concentration with an enhanced activity when the sugar surfactant is used as co-surfactant.
ISSN	09476539
e-ISSN	15213765
Journal	Chemistry - A European Journal
Issue Number	6
Volume Number	21
Language	English
Publisher	Wiley-VCH;ChemPubSoc Europe
Publisher Date	2015-02-02
Publisher Place	Germany
Access Restriction	Open
Subject Keyword	Candida Enzymology Emulsions Chemistry Fungal Proteins Metabolism Lipase Biocatalysis Esters Glycerylphosphorylcholine Analogs & Derivatives Hydrolysis Hydrophobic And Hydrophilic Interactions Kinetics Substrate Specificity Surface-Active Agents Temperature Research Support, Non-U.S. Gov't
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Catalysis

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