Akademik Veri Yönetim Sistemi
ENERGY SOURCES PART A-RECOVERY UTILIZATION AND ENVIRONMENTAL EFFECTS, cilt.36, sa.11, ss.1203-1211, 2014 (SCI-Expanded)
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.