关键词: 乙酰化, 花生球蛋白, 脂肪酶, 固定化, 蛋白载酶颗粒

Abstract:

Lipases are currently commonly used in the food industry for the modification of oils and fats， such as esterification and transesterification. In order to improve the chemical stability， thermal stability， and reusability of lipases， glutaraldehyde （GDA） was used as a crosslinking agent to crosslink lipase with acetylated arachin particles （AAPs）. And the immobilization efficiency and specific activity of protein carrier enzyme particles （lipase-AAPs） were optimized. The results showed that when the addition amount of succinic anhydride was 30% of the dry base mass of protein （the degree of acetylation was 41.71%±0.01%）， the GDA concentration was 1.0%， the crosslinking time was 1 h， the lipase concentration was 10%， and the lipase to particle ratio was 1∶4， the optimal immobilization efficiency and specific activity of lipase-AAPs were 12.95%±0.03% and 1.74±0.07 U·mg^-1， respectively. Micromorphological observation of lipase before and after crosslinking was performed using scanning electron microscopy （SEM）. Characterization of interactions between protein and lipases was measured by fourier transform infrared spectroscopy （FTIR）. In this paper， a method for the preparation of protein-loaded enzyme particles was provided， which was expected to provide theoretical and technical support for natural organic macromolecules as lipase carriers and avoid the safety problems caused by inorganic and organic synthetic particles.

Key words: acetylation, arachin, lipase, immobilization, lipase-AAPs