Enzyme-catalyzed resolution of racemate using enzyme functionalized silica nanoparticles in the presence of surfactants
- Authors
- Song, Yoon Seok; Lee, Hee Uk; Lee, Jong Ho; Park, Chulhwan; Kim, Seung Wook
- Issue Date
- 3월-2011
- Publisher
- ELSEVIER SCI LTD
- Keywords
- Lipase; Resolution; Naproxen; Surfactant; Silica nanoparticle; Immobilization
- Citation
- PROCESS BIOCHEMISTRY, v.46, no.3, pp.817 - 820
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROCESS BIOCHEMISTRY
- Volume
- 46
- Number
- 3
- Start Page
- 817
- End Page
- 820
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/113031
- DOI
- 10.1016/j.procbio.2010.12.010
- ISSN
- 1359-5113
- Abstract
- The enzyme-catalyzed resolution of racemic naproxen 2,2,2-trifluoroethyl thioester was performed by the immobilization of lipase on silica nanoparticles using a covalent bonding method. To increase the conversion and reaction rate of this resolution, we investigated the effect of non-ionic surfactants (M-SA 1025 and SM 20). The optimal reaction conditions such as temperature and loading amount of immobilized lipase were also determined. The addition of M-SA 1025 resulted in the increase in reaction rate (V-S), conversion (X-S) and enantioselectivity (E value) comparison with SM 20 and the control. The reaction performed in a mixture containing M-SA 1025 at 50 degrees C with 80 U/mL of immobilized lipase markedly improved the resolution of racemic naproxen 2,2,2-trifluoroethyl thioester compared to other conditions. (C) 2010 Elsevier Ltd. All rights reserved.
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Collections - College of Engineering > Department of Chemical and Biological Engineering > 1. Journal Articles
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