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HERO ID
2283430
Reference Type
Journal Article
Title
Pentynyl dextran as a support matrix for immobilization of serine protease subtilisin Carlsberg and its use for transesterification of N-acetyl-L-phenylalanine ethyl ester in organic media
Author(s)
Tahir, MN; Cho, E; Mischnick, P; Lee, JY; Yu, JH; Jung, S
Year
2014
Is Peer Reviewed?
Yes
Journal
Bioprocess and Biosystems Engineering
ISSN:
1615-7591
EISSN:
1615-7605
Publisher
Springer Verlag
Volume
37
Issue
4
Page Numbers
687-695
Language
English
PMID
23978850
DOI
10.1007/s00449-013-1038-8
Web of Science Id
WOS:000334930800011
Abstract
In this study, serine protease (subtilisin Carlsberg) was immobilized on pentynyl dextran (PyD, O-alkynyl ether of dextran, 1) and used for the transesterification of N-acetyl-L-phenylalanine ethyl ester (2) with different aliphatic (1-propanol, 1-butanol, 1-pentanol, 1-hexanol) and aromatic (benzyl alcohol, 2-phenyl ethanol, 4-phenyl-1-butanol) alcohols in tetrahydrofuran (THF). The effect of carbon chain length in aliphatic and aromatic alcohols on initial and average transesterification rate, transesterification activity of immobilized enzyme and yield of the reaction under selected reaction conditions was investigated. The transesterification reactivity of the enzyme and yield of the reaction increased as the chain length of the alcohols decreased. Furthermore, almost no change in yield was observed when the immobilized enzyme was repeatedly used for selected alcohols over six cycles. Intrinsic fluorescence analysis showed that the catalytic activity of the immobilized enzyme in THF was maintained due to retention of the tertiary structure of the enzyme after immobilization on PyD (1).
Keywords
Enzyme catalysis; Immobilization; N-acetyl-L-phenyl ethyl ester; Pentynyl dextran; Subtilisin Carlsberg; Transesterification
Tags
IRIS
•
n-Butanol
Database searches
Pubmed
Database Searches - March 2014 (private)
Pubmed - 3/2014
Excluded (not pertinent)
Use in sample prep or assay
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