N-acylation of L-amino acids in aqueous media: Evaluation of the catalytic performances of Streptomyces ambofaciens aminoacylases

• Published in: Enzyme and microbial technology 2020-06, Vol.137, p.109536-109536, Article 109536
• Main Authors: Bourkaib, Mohamed Chafik, Delaunay, Stephane, Framboisier, Xavier, Hôtel, Laurence, Aigle, Bertrand, Humeau, Catherine, Guiavarc’h, Yann, Chevalot, Isabelle
• Format: Article
• Language: English
• Subjects: Amino-Acid-Based; Aminoacylases; Biocatalysis; Enzymatic N-acylation; Life Sciences; Selectivity; Streptomyces ambofaciens; Surfactant
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/j.enzmictec.2020.109536

[Display omitted] •Large spectrum of N-acylation activity toward the amino acids of the extracted aminoacylases from S. ambofaciens.•Influence of side chain of the acyl receiver on the reactivity of the aminoacylases.•Evidence that the aminoacylase (Sam-AA) is responsible of the major N-α-acylation activity.•Different affinity and reactivity of the enzyme with the acyl receiver and the acyl donor.•Improvement of the catalytic performance using Cobalt as divalent ion. N-acylated amino acids are widely used as surfactants and/or actives in cosmetics and household formulations. Their industrial production is based on the use of the Schotten-Baumann chemical and unselective reaction. Faced to the growing demand for greener production processes, selective enzymatic synthesis in more environment-friendly conditions starts to be considered as a potential alternative. This study concerns the use of the aminoacylases from Streptomyces ambofaciens to selectively catalyse aminoacid acylation reaction by fatty acids in aqueous medium. The results demonstrated that, when using undecylenoic acid as acyl donor, these aminoacylases properly catalyse the acylation of 14 of the 20 proteogenic l-amino acids tested on their α amino group with a great variability depending on the nature of the amino acid (polar or not, positively/negatively charged, aromatic or not…). More precisely, the following 9 amino acids were shown to be preferentially acylated by S. ambofaciens aminoacylases as follows: lysine > arginine > leucine > methionine > phenylalanine > valine > cysteine > isoleucine > threonine. Different fatty acids were used as acyl donors and, in most cases, the fatty acid length influenced the conversion yield. The kinetic study of α–lauroy-lysine synthesis showed a positive influence of lysine concentration with Vmax and Km of 3.7 mM/h and 76 mM, respectively. Besides, the lauric acid had an inhibitory effect on the reaction with Ki of 70 mM. The addition of cobalt to the reaction medium led to a more than six-fold increase of the reaction rate. These results, achieved with the aminoacylases from S. ambofaciens represent an improved enzyme-based N-acylated amino acids production in order to provide an alternative way to the Schotten-Baumann chemical reaction currently used in the industry.