The use of
enzymes and biotechnology appears to be quite attractive as an alternative to the classical chemical operations in a variety of useful organic compounds preparations due to the milder operational conditions they require. However, the use of enzymes has been limited due to the low
stability and
catalytic efficacies of enzymes in their native form. Considering this, many attempts have been made to improve their catalytic properties in promoting enzymes
stabilities and activities. This includes restriction of
lipase onto
solid materials or immobilization of lipase. In this study, seven types of solid materials ranging from mineral clay (hydrotalcite) to polymers were used to immobilize lipase from Candida rugosa. The physical properties of the solid materials were compared in terms of pore size, surface area, polarity and adsorption capacity and their effects on the stability and activity of the lipase
immobilized onto them. Stabilities and activities of lipase immobilized onto various solid materials were determined according to their catalytic efficacies in the
esterification reaction between (±)-menthol and butyric anhydride. Lipase from Candida rugosa was found to bind most (72 – 73 % immobilization) onto solid materials with larger pore sizes and adsorption capacities (Eupergit C and C250L). On the other hand, high yields of (-)-menthyl butyrate (~ 40 – 60 %) which imply the high stabilities and activities of lipase, was achieved when lipase immobilized onto polar solid materials (Amberlite XAD7, Eupergit C and C250L; and hydrotalcite) were employed.
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