Ester Synthesis by a Recombinant Cutinase in Reversed Micelles of a Natural Phospholipid

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Abstract
Fusarium solani pisi recombinant cutinase solubilized in reversed micelles of a nonionic surfactant (phosphatidylcholine) in isooctane was used to catalyze the esterification of fatty acids with 2-butanol. Various parameters affecting the catalytic activity of the microencapsulated cutinase, such as pH, wo (molar ratio water/surfactant), temperature and substrate concentration were investigated. Maximal specific activity were obtained with wo=13, at pH 10.7 and 35d`C. The cutinase showed a higher specific activity for short length fatty acids, namely butyric acid. Calculation of the apparent kinetic parameters (km and Vmax) for the synthesis of butyl butyrate, showed a low apparent affinity of the cutinase in phosphatidylcholine reversed micelles for both substrates.