生物加工过程2019，Vol.17Issue(2)：159-165,7.DOI:10.3969/j.issn.1672-3678.2019.02.007
D-泛解酸内酯水解酶的固定化及酶学性质
Immobilization and characterization of D-lactonohydrolase
摘要
Abstract
To improve the efficiency of D-lactonohydrolase, the most suitable carrier was selected to immobilize the enzyme.The immobilization conditions were optimized.At the same time, the optimal reaction conditions and enzymatic properties of the immobilized enzyme were studied.The best immobilized carrier was resin D380 and the optimal conditions for immobilization were as follows:enzyme adsorption amount was 30 U per gram wet resin, adsorption pH was 7.0, adsorption temperature was 30 ℃, adsorption time was 5 h. At a concentration of 0.1％ for glutaraldehyde and 1 h for glutaraldehyde crosslinking, the specific enzyme activity of the immobilized enzyme was (11.5±0.12) U/g under optimal conditions. The optimal reaction temperature of the immobilized D-lactonohydrolase was 37 ℃, and the optimal pH was 7.5.The kinetic constants of the free enzyme and the immobilized enzyme were 170.25 and 207.60 mmol/L, respectively.The immobilized enzyme was activated by Ca2+, and inhibited by Mn2+.关键词
D-泛解酸内酯水解酶/固定化酶/动力学常数Key words
D-lactonohydrolase/immobilized enzyme/kinetic constants分类
生物科学引用本文复制引用
王开放,张梁,辛瑜,曾伟,丁重阳,石贵阳..D-泛解酸内酯水解酶的固定化及酶学性质[J].生物加工过程,2019,17(2):159-165,7.基金项目
江苏省科技计划(产业前瞻与共性关键技术竞争项目)(BE2018055) （产业前瞻与共性关键技术竞争项目）
