Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: effect on the enzymatic activity in solvent-free ethyl oleate synthesis

• Published in: Enzyme and microbial technology 2005-02, Vol.36 (2), p.338-349
• Main Authors: Foresti, M.L., Alimenti, G.A., Ferreira, M.L.
• Format: Article
• Language: English
• Subjects: Adsorbed lipase; Bioimprinting; Biological and medical sciences; Biotechnology; Candida rugosa; Fundamental and applied biological sciences. Psychology; Immobilization of enzymes and other molecules; Immobilization techniques; Interfacial activation; Methods. Procedures. Technologies
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/j.enzmictec.2004.09.012

Lipase from Candida rugosa adsorbed on polypropylene powder (CR/PP) was subjected to activation pre-treatments in order to enhance its activity in solvent-free ethyl oleate synthesis. The lipase activation achieved upon adsorption onto a hydrophobic support like PP was further enhanced through oil–water interfacial activation and bioimprinting of the immobilized catalyst. Several aliphatic hydrocarbons/buffer pH 7 mixtures were used in the pre-activation of CR/PP with specific activity increments of up to 29%. Molecular bioimprinting was also performed, with specific activity enhancement of near 70% with respect to non-treated CR/PP. The effect of several fatty acids used as templates and the water present in the reaction medium was studied. The oil–water activation and bioimprinting treatments that led to the best activities were assayed at the immobilization step. Instead of pre-treating CR/PP adsorbed in buffer medium, interfacial activation with octane/buffer and bioimprinting with a mix of fatty acids were carried out in the immobilization vial. The best results were found for CR/PP immobilized in 5/95 octane/buffer (v/v, %) medium. In that way, a biocatalyst with enhanced specific activity is obtained right from the immobilization vial with no need of further activation steps prior to reaction.