Enzymatic acylation of polar dipeptides: Influence of reaction media and molecular environment of functional groups |
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Authors: | Eric Husson Catherine Humeau Cédric Paris Régis Vanderesse Xavier Framboisier Ivan Marc Isabelle Chevalot |
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Institution: | 1. LSGC, Nancy Université, CNRS, 2 avenue de la forêt de Haye- 54500 Vandoeuvre-lès-Nancy, France;2. LBB, Nancy Université, 2 avenue de la forêt de Haye- 54500 Vandoeuvre-lès-Nancy, France;3. LCPM, Nancy Université, CNRS-URA 494, BP 451, F-54001 Nancy Cedex, France |
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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 N?-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. |
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