Abstract
The immobilization of Rhizopus oryzae lipase (RoL) by hydrophobic adsorption on polypropylene supports with additives was investigated. Additives such as hen egg albumin, sodium caseinate and CAVAMAX® W6 were used to coat the support during immobilization where the immobilized RoL on coated support was compared to those of noncoated support. Following the immobilization, the catalytic activity of immobilized RoL was characterized based on different temperatures and pH. The immobilized RoL without additives showed optimal lipase activity at an optimum temperature of 50 °C and pH 6. However, RoL lipase that was immobilized on support treated with CAVAMAX® W6 had better performance in terms of hydrolytic activity and stability as compared to other additives. In addition, by having a support treated with hen egg albumin, the immobilized RoL was capable of yielding higher ester during esterification reactions.
Highlights
IntroductionLipases (triacylglycerol hydrolases, EC 3.1.1.3) belong to the enzyme class of hydrolases catalyzing the hydrolysis of the triglycerides at the lipid water interface into fatty acids, mono- and diacylglycerols, and glycerol
Lipases belong to the enzyme class of hydrolases catalyzing the hydrolysis of the triglycerides at the lipid water interface into fatty acids, mono- and diacylglycerols, and glycerol
Hen egg albumin was used as an additive in the immobilization of Rhizopus oryzae lipase (RoL) according to Bosley and Peilow, 1993 [14]
Summary
Lipases (triacylglycerol hydrolases, EC 3.1.1.3) belong to the enzyme class of hydrolases catalyzing the hydrolysis of the triglycerides at the lipid water interface into fatty acids, mono- and diacylglycerols, and glycerol. Lipases have been widely used in the food industry and have a highly selective reaction towards a wide range of substrates. Said lipases are highly unstable in an aqueous form, which requires immobilization to form immobilized lipase with enhanced activity, thermal, reusability, and operational stability. Various immobilization methods have been applied to lipase, such as adsorption, entrapment, covalent binding, and crosslinking in which the most applied method for lipase immobilization is physical adsorption. The interaction between support and lipase via physical adsorption is weak and prone to leaching out from the supports [2,3]
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