Optimum immobilization of Candida rugosa lipase on Celite by RSM

Immobilization of Candida rugosa lipase (lipase AY-30) by adsorption on Celite led to a markedly improved performance of the enzyme. Immobilization conditions and characterization of the immobilized enzyme were investigated. Lipase activity was measured with glycerol tributyrate as substrate. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (30–90 min), immobilization temperature (0–20 °C), and enzyme/support ratio (0.3–0.5, w/w), on the specific activity of immobilized lipase. Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 59.1 min, immobilization temperature 10.7 °C, and enzyme/support ratio 0.5 (w/w); the highest specific activity obtained was 18.16 U/mg-protein with activity yield of 34.1%.