Yucel, Y.Demir, C.Dizge, N.Keskinler, B.2024-09-182024-09-1820141556-70361556-7230https://doi.org/10.1080/15567036.2010.545805https://hdl.handle.net/20.500.12483/10951In 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.eninfo:eu-repo/semantics/closedAccesslipase immobilizationbiodieselNovozyme 388alcoholysistransesterificationLipozyme TL-100LArticle36111203121110.1080/15567036.2010.5458052-s2.0-84898068648Q1WOS:000333875400007Q4