| Literature DB >> 33225381 |
Qiong Yang1,2, Liuying Li3, Bochu Wang4, Liancai Zhu3, Jun Tan5.
Abstract
7α-Hydroxysteroid dehydrogenase (7α-HSDH) is one of the key enzymes in the catalytic reaction of taurochenodeoxycholic acid (TCDCA). To improve the activity of immobilized 7α-HSDH, the microenvironment of immobilized 7α-HSDH was modified with epoxy resin and ethanediamine (EDA). The amino-epoxy support was characterized by Fourier transform infrared (FTIR), Spectrometer elemental analysis (EA), scanning electron microscopy (SEM), contact angle (CA), and Zetasizer. The effects of the immobilization of 7α-HSDH on the amino-epoxy resin and epoxy resin were studied. The results indicated that the relative activity of immobilized 7α-HSDH on the amino-epoxy resin increased by approximately 80%. Meanwhile, the immobilized 7α-HSDH showed favorable thermal stability and operational stability. The thermal stability of immobilized 7α-HSDH increased at temperatures ranging from 15 to 35 °C, while the relative activities of 7α-HSDH immobilized on the amino-epoxy resin and epoxy resin retained 56.4% and 61.0%. After 6 cycles, the residual activities of the 7α-HSDH immobilized on the amino-epoxy resin and epoxy resin were 81.4% and 89.5%, respectively.Entities:
Keywords: 7α-Hydroxysteroid dehydrogenases; Epoxy resin; Immobilization; Microenvironment; Modification
Mesh：
Substances：
Year: 2020 PMID： 33225381 DOI： 10.1007/s12010-020-03473-w
Source DB: PubMed Journal: Appl Biochem Biotechnol ISSN： 0273-2289 Impact factor: 2.926