| Abstract [eng] |
Bacterial lipolytic enzymes (carboxylesterases, EC 3.1.1.1 and triacylglycerol acylhydrolases, EC 3.1.1.3) form a large group of physiologically relevant enzymes and are also well known for their use in multiple biotechnology sectors. The wide variety of applications of these enzymes has led to the increased development of research in order to characterize them and achieve lipolytic enzymes with improved properties through protein engineering, immobilization, etc. Currently, lipolytic enzymes remain as one of the most widely used enzymes to replace traditional industrial processes. Also, despite the high number of bacterial lipolytic enzymes identified, only a small portion are experimentally studied. In the present work, lipolytic enzymes (LipBST and EstAG1) of two bacterial strains identified as Bacillus stratosphericus and Staphylococcus saprophyticus were analyzed. LipBST was identified as a lipase having a minimal α/β-hydrolase fold with functional properties suitable for biodegradation of various fatty substances. Different physical and chemical properties of LipBST were improved by immobilization on hydrophobic support; enzymatic preparation was assessed as suitable for the catalysis of transesterification reactions in anhydrous media. Another enzyme studied in this work –EstAG1 esterase - was determined to be unique lipolytic enzyme in terms of its amino acid (a.a) sequence and atypical conservative regions. Based on the a.a sequence peculiarities and phylogenetic position of EstAG1, it has been assigned to be a member of a new family of bacterial lipolytic enzymes. |
