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

• Published in: Chemistry - A European Journal
• Main Authors: Steudle, Anne K., Subinya, Mireia, Nestl, Bettina M., Stubenrauch, Cosima
• Other Authors: EPRSC
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2014
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1002/chem.201405335; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fchem.201405335; https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201405335

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.