Hydrolysis of Hydrophobic Esters in a Bicontinuous Microemulsion Catalysed by Lipase B from Candida antarctica |
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| Authors: | Anne K. Steudle Dr. Mireia Subinya Dr. Bettina M. Nestl Prof. Dr. Cosima Stubenrauch |
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| Affiliation: | 1. Chemistry Department, Durham University, South Road, DH1 3LE Durham (UK);2. Institute of Physical Chemistry, University of Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart (Germany);3. Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart (Germany) |
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| 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 CiEj 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‐C10G1). 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. |
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| Keywords: | biocatalysis enzymes esters hydrolases hydrolysis |
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