Enhanced stability and reusability of marine epoxide hydrolase using ship-in-a-bottle approach with magnetically-separable mesoporous silica

Young Hyun Kim, Inseon Lee, Sung Hee Choi, Ok Kyung Lee, Jongmin Shim, Jinwoo Lee, Jungbae Kim, Eun Yeol Lee

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)48-51
Number of pages4
JournalJournal of Molecular Catalysis B: Enzymatic
Volume89
DOIs
Publication statusPublished - 2013 May

Bibliographical note

Funding Information:
This work was supported by the Marine and Extreme Genome Research Center Program , Ministry of Land , Transportation and Maritime Affairs, Republic of Korea . This work was also supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (No. 2012K001385 ).

Keywords

  • Enzyme immobilization
  • Epoxide hydrolase
  • Mesoporous silica
  • Mugil cephalus
  • Nanoscale enzyme reactor

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

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