This paper, completed by a research scholar at the College of Chemistry and Chemical Engineering of Yunnan Normal University, discusses papers on the study of lipase bio-imprinting and cross-linking, published in the important journal .

In this paper, lipase was used as the imprinting object. The lipase was firstly bio-imprinted, then the lipase of the imprinted enzyme was acetylated and cross-linked, and the acylation and cross-linking were detected by trinitrobenzenesulfonic acid (TNBS). degree. The results showed that the number of free amino groups decreased after acylation and cross-linking, indicating that some amino groups were involved in acetylation, which made the cross-linking of the imprinted enzyme possible. At the same time, the cross-linked enzyme was structurally stable, not easy to be inactivated, and the activity was significantly higher than that of acetylase.

15 mg of lipase was dissolved in 0.5 mL of hexane solution and shaken to obtain a suspension. 0.25 mL of crosslinker EDMA and 4 mg of initiator azobisisobutyronitrile (AIBN) were added to the suspension, at 4 ° C, 366 The nm light was irradiated for 5 h to cause copolymerization. The copolymer was washed 3 times with 0.5 mL of hexane, and finally the cross-linked blotting enzyme was vacuum dried for 2 hours to obtain a cross-linked blotting enzyme (CLIE).