Wang Ziqiang, Su Munan, Li Yanliang, Wang Yunshan, Su Zhiguo
State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, China.
Biotechnol Lett. 2017 Dec;39(12):1859-1863. doi: 10.1007/s10529-017-2419-x. Epub 2017 Sep 5.
To investigate the expression and immobilization of recombinant cis-epoxysuccinate hydrolase (ESH), and its application in the biological production of L-(+)-tartaric acid.
E. coli BL21 (DE3)/pET11a-ESH (His) was engineered to express recombinant ESH. The enzyme had an activity of 262 U mg. The recombinant ESH was immobilized on agarose Ni-IDA matrix with metal ion affinity interaction to improve its thermostability and pH stability. The immobilization efficiency and activity yield were 94 and 95%, respectively. The specific catalytic efficiency of immobilized ESH was 104 mg U h during the continuous enzymatic production process.
ESH with a histidine tag was immobilized and used for the continuous production of L-(+)-tartaric acid.
研究重组顺式环氧琥珀酸水解酶（ESH）的表达、固定化及其在L-(+)-酒石酸生物生产中的应用。
构建大肠杆菌BL21(DE3)/pET11a-ESH(His)表达重组ESH。该酶活性为262 U mg。通过金属离子亲和作用将重组ESH固定在琼脂糖镍-亚氨基二乙酸基质上，以提高其热稳定性和pH稳定性。固定化效率和活性回收率分别为94%和95%。在连续酶促生产过程中，固定化ESH的比催化效率为104 mg U h。
固定化带有组氨酸标签的ESH用于L-(+)-酒石酸的连续生产。
