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    Methods for Lipase Immobilization and Their Use for Biodiesel Production from Vegetable Oil
    (Taylor & Francis Inc, 2014) Yucel, Y.; Demir, C.; Dizge, N.; Keskinler, B.
    In the present work, two different lipases (triacylglycerol hydrolase, EC 3.1.1.3), Lipozyme TL-100L and Novozyme 388, were immobilized onto three different low-cost supports using both adsorption and covalent method: celite 545, silica gel, and styrene-divinylbenzene copolymer. The maximum immobilization yield was obtained as 79.0% for Lipozyme TL-100L and the highest specific activity was 6.5 U/mg protein for Novozym 388. The properties of the support and immobilized derivatives were characterized by Fourier transform infrared spectroscopy. Maximum methyl esters yield was obtained as 98.3%. The lipases, which are immobilized by covalently, proved to be stable after even 10 repeated reuses.
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    The Optimization of Immobilized Lipase-catalyzed Transesterification of Canola Oil by Response Surface Methodology and Mixture Design
    (Taylor & Francis Inc, 2012) Yucel, Y.; Demir, C.
    The abilities of three immobilized lipases from Candida Antarctica (Novozym 435), Thermomyces lanuginosus (Lipozyme TL-IM), and Rhizomucor miehei (Lipozyme RM-IM) to catalyze the transesterification of canola oil with methanol were investigated. Response surface methodology and central composite design were employed to optimization of the reaction parameters. Simplex lattice mixture design was employed to evaluate the effect of the composition of lipase mixtures on the yield of transesterification reaction. The highest conversion of canola oil to fatty acid methyl ester was obtained as 97.2%. Mixture of lipases could be used to obtain higher conversion of canola oil to biodiesel.