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HERO ID
7744855
Reference Type
Journal Article
Title
The Activity of Rhizomuchor miehei Lipase as a Biocatalyst in Enzymatic Acylation of Cyclic Alcohol
Author(s)
Iftitah, ED; Srihardyastuti, A; Ariefin, M; AIP
Year
2017
Is Peer Reviewed?
Yes
Journal
AIP Conference Proceedings
ISSN:
0094-243X
EISSN:
1551-7616
Publisher
American Institute of Physics Inc.
Book Title
AIP Conference Proceedings
Volume
1823
Language
English
DOI
10.1063/1.4978190
Web of Science Id
WOS:000404123700117
Abstract
We report the activity of Rhizomuchor miehei lipase (RML) as a biocatalyst, in particular the investigations concerning the effort of substrate-structure reactivity on the enzymatic acylation. The acylation was studied using acetic anhydride as an acyl donor and performed in n-hexane as a solvent. The selectivity of the enzymatic acylation was revealed by Gas Chromatography-Mass Spectra. We observed that, RML has shown different behavior when catalyzing the acylation of isopulegol and mixture of isopulegol and citronellal (ratio 1:1). The chemoselectivity for the O-acylation was improved when the acyl acceptor included mixture of isopulegol and citronellal. © 2017 Author(s).
Editor(s)
Purwiandono G.
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