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  • Title: Hydrolysis of hydrophobic esters in a bicontinuous microemulsion catalysed by lipase B from Candida antarctica.
    Author: Steudle AK, Subinya M, Nestl BM, Stubenrauch C.
    Journal: Chemistry; 2015 Feb 02; 21(6):2691-700. PubMed ID: 25512180.
    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 Ci Ej 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-C10 G1 ). 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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