Development of magnetically separable immobilized lipase by using cellulose derivatives and their application in enantioselective esterification of ibuprofen
- Authors
- Gowoun, Lee; Joo, Hongil; Kim, Jungbae; Lee, Jung-Heon
- Issue Date
- 3월-2008
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- enzyme stabilization; ibuprofen; racemic resolution
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.18, no.3, pp.465 - 471
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 18
- Number
- 3
- Start Page
- 465
- End Page
- 471
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/124028
- ISSN
- 1017-7825
- Abstract
- Highly active, stable, and magnetically separable immobilized enzymes were developed using carboxymethyl cellulose (CMC) and diethylaminoethyl cellulose DEAE-C; hereafter designated "DEAE" as supporting materials. Iron oxide nanoparticles penetrated the micropores of the supporting materials, rendering them magnetically separable. Lipase (LP) was immobilized on the surface of the supporting materials by using cross-linked enzyme aggregation (CLEA) by glutaraldehyde. The activity of enzyme aggregates coated on DEAE was approximately 2 times higher than that of enzyme aggregates coated on CMC. This is explained by the fact that enzyme aggregates with amine residues are more efficient than those with carboxyl residues. After a 96-h enantioselective ibuprofen esterification reaction, 6% ibuprofen propyl ester was produced from the racemic mixture of ibuprofen by using DEAE-LP, and 2.8% using CMC-LP.
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Collections - College of Engineering > Department of Chemical and Biological Engineering > 1. Journal Articles
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