Abstract: To improve the synthetic effect of cinnamyl acetate, Pseudomonas cepacia lipase was immobilized on cotton fibers in a column glass bottle to form a facile bioreactor and used to catalyze transesterification between cinnamyl alcohol and vinyl acetate. The results were that the bioreactor could transform 92% of substrate after 12 h at 37 ℃ and 160 r/min while native lipase only gave a conversion of 35% under the same reaction conditions. Even at static state, the bioreactor brought high conversions, which were 88%, 84% and 44% after 12 h at 37, 25 and 4 ℃, respectively. In repeated 6 h catalysis, the immobilized and native lipases exhibited that the decrease rates in ability of transforming substrate were 0.3% and 0.5% per hour. It showed that the immobilized lipase in bioreactor behaved activity and stability higher than native lipase in the non-aqueous phase, which was also so at static state. This meant that it was a type of effectively low-carbon immobilized lipase bioreactor.

Key words: cinnamyl acetate, lipase, absorbent cotton, enzyme activity, enzyme stability