Enhanced stability and reusability of marine epoxide hydrolase using ship-in-a-bottle approach with magnetically-separable mesoporous silica
SCIE
SCOPUS
- Title
- Enhanced stability and reusability of marine epoxide hydrolase using ship-in-a-bottle approach with magnetically-separable mesoporous silica
- Authors
- Kim, YH; Lee, I; Choi, SH; Lee, OK; Shim, J; Lee, J; Kim, J; Lee, EY
- Date Issued
- 2013-05
- Publisher
- ELSEVIER SCIENCE BV
- Abstract
- We developed magnetically-separable and highly-stable biocatalyst system of Mugil cephalus epoxide hydrolase (McEH) for enantioselective hydrolysis of racemic epoxides. McEH protein was adsorbed and cross-linked into mesoporous silica with bottle-neck mesopores, which effectively prevented the leaching of cross-linked McEH in a larger mesocellular pores. This ship-in-a-bottle approach allows for highly loaded and stable McEH system. For example, free McEH showed only 7.5% of initial activity under shaking condition at 80 h while ship-in-a-bottled McEH retained 79.5% of initial activity in the same condition. Stable McEH in magnetically-separable mesoporous silica could achieve the yield of 45% for the preparation of enantiopure (S)-styrene oxide with 98%ee. The magnetic nanoparticles pre-incorporated in mesoporous silica enabled an easy recovery of immobilized McEH for repetitive batch resolutions of racemic styrene oxide, allowing for more than 50% of the initial activity was retained after seven recycled uses. (C) 2012 Elsevier B.V. All rights reserved.
- Keywords
- Epoxide hydrolase; Mugil cephalus; Nanoscale enzyme reactor; Mesoporous silica; Enzyme immobilization; MUGIL-CEPHALUS; IMMOBILIZATION; STABILIZATION; NANOPARTICLES; IMPROVEMENT; CATALYSIS; ENZYMES; SYSTEM
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/14815
- DOI
- 10.1016/J.MOLCATB.2012.12.012
- ISSN
- 1381-1177
- Article Type
- Article
- Citation
- JOURNAL OF MOLECULAR CATALYSIS B: ENZYMATIC, vol. 89, page. 48 - 51, 2013-05
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