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Enzymatic acylation of polar dipeptides: Influence of reaction media and molecular environment of functional groups

Paper ID Volume ID Publish Year Pages File Format Full-Text
35550 45095 2009 7 PDF Available
Title
Enzymatic acylation of polar dipeptides: Influence of reaction media and molecular environment of functional groups
Abstract

The enzymatic acylation of polar dipeptides was investigated. First, the Novozym435®-catalyzed acylation of Lys-Ser, HCl exhibiting three potential acylable sites was carried out in organic media (2-methyl-2-butanol, oleic acid) and in an ionic liquid ([Bmim]+[PF6]−). In these reactions, the chemo-selectivity of the acylation was exclusively in favour of the Nɛ-lysine acylation and the efficiency (substrate conversion) was demonstrated to be under control of the peptide solubility. The use of [Bmim]+[PF6]− permitted to significantly improve the dipeptide solubility, and to enhance both substrates conversion and initial rates of acylation reaction. In the three reaction media used, the O-acylated derivative of the dipeptide was never detected suggesting a weak reactivity of the serine hydroxyl group due to its molecular environment and particularly to the presence of a free carboxylic group known for its electroattractor property.Last, the acylation of a natural dipeptide (carnosine), exhibiting a very low solubility in organic solvents, was also performed. Carnosine was successfully N-acylated in 2-methyl-2-butanol, and a yield of 39% was obtained when improving the substrate solubility: a better dispersibility was obtained by application of a high pressure on the reaction medium just before starting the reaction.

Keywords
N-acylation; Lipase CALB; Dipeptide; Carnosine; Organic solvent; Ionic liquid
First Page Preview
Enzymatic acylation of polar dipeptides: Influence of reaction media and molecular environment of functional groups
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 4, April 2009, Pages 428–434
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering