Abstract: In order to effectively catalyze the synthesis of cinnamyl acetate as an essence, it is necessary to enhance the nonaqueous stability of enzymes. The usual method is to prepare a native enzyme into an enzyme immobilized in some carriers. This article investigates the effects of two types of carriers on the catalytic activity of the lipase. Pseudomonas cepacia lipase selected as a biocatalyst, copper phthalocyanine and absorbent cotton as carriers, immobilized lipase was prepared through physical adsorption. The immobilized lipase was used to catalyze the transesterification reaction between cinnamyl alcohol and vinyl acetate. It was found that when preparing immobilized enzymes, the ideal dosage of copper phthalocyanine as a single carrier was 10 mg, and the ideal dosage of absorbent cotton as a single carrier was 25 mg when the enzyme dosage was 10 mg. The ideal dosage of both carriers when used simultaneously was also 10 mg and 25 mg, respectively. The prepared dual carrier immobilized lipase showed a decrease of less than 1% in the ability of the immobilized enzyme to convert substrates and a decrease of 23% in the ability of native lipase to convert substrates during multiple repeated catalytic transesterification reactions. It means that the dual carrier immobilized lipase behaves fine nonaqueous stability and has industrial application potential.

Key words: lipase, immobilization, enzyme activity, enzyme stability, cinnamyl acetate