Stability and Esterification Activity of Candida rugosa Lipase Immobilized on Celite with Acetone Solvent

Abstract

Candida rugosa lipase (CRL) is an enzyme that is widely used in biopharmaceutical and biopesticide industries due to its high catalytic ability and reusability. However, conditions from industrial processes that are often outside CRL stability range may cause denaturation or destabilization of the enzyme, causing it to be not reusable, hence lowering its economic value. To increase its catalytic activity, stability, and reusability, CRL enzyme can be immobilized in a matrix. In this study, the CRL was physically adsorbed onto Celite-545. The immobilization process was done using buffer solution with the addition of acetone. The influence of initial enzyme concentration and immobilization condition (time, temperature, and pH) were optimized using OFAT method. The data were taken in terms of esterification activity, thermal stability, and protein content. The result showed good thermal stability of the immobilized biocatalysts and an increase in esterification activity at optimum conditions that supported the efficiency of Celite-545 as lipase immobilization supports.