Elvina Dhiaul Iftitah, Arie Srihardyastuti, Mokhamat Ariefin
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).
Chemistry Department, Faculty of Science, University of Brawijaya, Jl. Veteran Malang, Indonesia; Pureaa, Institute of Essential Oil, University of Brawijaya, Malang, Indonesia
