Lipases, Definition, and their Application
Journal Title: IOSR Journal of Pharmacy and Biological Sciences (IOSR-JPBS) - Year 2017, Vol 12, Issue 3
Abstract
Esterase and lipase have been consisted of α/β hydroxylase super family that characterized primarily by their α/β hydroxylase fold (common fold), which is in the center, pre-dominantly parallel β-sheet and flanked via the connections of α-helical. Nucleophilic elbow is an esterases and lipases that shared the characteristic sequence motifs (GXSXG). The residues of these amino acids compose a triad of catalyse in the specific-order (serine – aspartic acid - histidine) in the chain of polypeptide. Consequently, the most of lipases and esterases resemble serine-proteases and lipases in hydrolytic mechanism. Esterases (EC 3.1.1.1), as well as lipases (EC 3.1.1.3) are the versatile classes of biocatalysts. Due to their region-, enatio-selectivity and high specificity. Esterases are those that can catalyze the hydrolysis of short-acyl-chain-lengthed triglycerides less than 10, whereas, lipases are catalysts that can hydrolyze long-acyl-chain-lengthed triglycerides more than 10. Lipases applications can widely produce from a bacterial and fungal production. Lipases applications and their biotechnology significant are presented in different field such as medical biotechnology, detergent industries, organic synthesis, biodiesel production, agrochemical industries, flavor industries, and food industries.
Authors and Affiliations
Waznah Moayd1, Yunjun Yan1*
Keywords
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