Immobilization of Lipase from Candida rugosa on Chitosan Beads for Transesterification Reaction

A.N Abd Alla,H.A Said,M Nasratun,A Noraziah

doi:10.3844/ajassp.2009.1653.1657

Abstract

Problem statement: Further study is recommended to improve the immobilization technique and the immobilized lipase’s performance as catalysis in transesterification reaction. Approach: To investigate the ability of immobilized lipase on chitosan beads to catalyze the transesterification of cooking oil to an ester. The porous bead of chitosan was used for immobilization of lipase from Candida rugosa by physical adsorption. Parameters like reaction time and oil to methanol molar ratios were studied to compare the transesterification performance between free lipase and immobilized lipase. Results: The experimental result showed that the maximum conversion of ester using immobilized lipase and free lipase were 72.25 and 76.5% respectively which was obtained at conditions of 1:4 molar ratios and reaction time of 48 h. Conclusion: Even though the conversion of ester was higher in free lipase than in immobilized lipase, it is still feasible to use immobilized lipase to catalyze the transesterification process provided it’s easier to separate the end product and high potential to be reused. Immobilize lipase also tolerated the water content of oil and increases product yield by avoiding the soap formation.

Highlights

Many efforts have been made over the years to develop the catalytic activity and operational stability of industrial enzymes through the use of genetic engineering, immobilization and/or process alterations
Immobilized lipase prepared in previous had been used as a catalyst for transesterification reaction that to Immobilized 1:4 lipase
The experiment results show that immobilized lipase has an optimum reaction time of 48 hours and the oil methanol ratio is 1:4

Summary

Introduction

Many efforts have been made over the years to develop the catalytic activity and operational stability of industrial enzymes through the use of genetic engineering, immobilization and/or process alterations. Lipases are widely used in industrial applications due to the wealth of reactions they catalyze. It is an important enzyme in biological systems, where it catalyzes the hydrolysis of triacylglycerol to glycerol and fatty acids[1]. Besides their natural substrates, lipases has unique characteristics such as can catalyze reactions involving insoluble organic and aqueous phases and are able to preserve their catalytic activity in organic solvents, biphasic system and in micellar solutions[2]. Versatility of lipase catalyzed reactions made them a unique heterogeneous catalyst for transesterification reactions

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