Conjugated linoleic acid‐producing enzymes: A bioinformatics study

Linoleic acid isomerases (LAI) are enzymes responsible for conversion of linoleic acid (LA) to conjugated linoleic acids (CLA) in different isomeric forms. CLAs are well known for numerous beneficial effects as functional foods. Despite identification of several LAI producing‐bacteria and release of their LAI nucleotide sequences to Bio‐Banks, no related bioinformatics study on these important enzymes is addressed yet. To gain insights into the structural/functional and phylogentic relations of LAIs as well as recombinant production of the desired enzyme, we employed several bioinformatical tools to analyze their primary structure and physicochemical properties. The results indicated that LAIs produced in different bacterial strains might be divided in two distinct families (Propionibacterium acnes and myosin cross‐reactive antigen (MCRA)‐like LAIs) with specific isomerase activities. In another part of the study, physicochemical properties, solubility upon over expression in E. coli, disulfide bond formation, and potential glycosylation sites in LAI sequences were predicted using bioinformatics tools and the most appropriate strategy for recombinant production of each LAI was determined. Our predicted data may be useful for further experimental studies toward production of the desired LAI.