In silico structural elucidation of novel lipase encoded by LipHim1 gene and it’s activation by Tween 60

Abstract

Lipases are unique enzymes which act on esters that catalyze both the hydrolysis of fats and the synthesis of fatty acid esters including acyl glycerides used in laundry, food, chemical, and also in pharmaceutical industries. Recently a novel LipHim1 gene was isolated from high diversified soil using metagenomic approach. Earlier studies revealed that lipases are capable of hydrolyzing fatty acid esters of polyoxyethylene sorbitan (Tweens) leaving turbidity on LB agar plate. Appearance of turbidity around spots inoculated with Tween 60 was traditionally measured as a function of lipase activity of extracellular including novel lipase encoded by LipHim1 gene. In this study, we have employed homology modelling to elucidate the structural aspects of LipHim1 gene encoded lipase enzyme. Furthermore, an In silico analysis employing molecular docking and molecular dynamic simulations study was taken up to reveal molecular level interactions responsible for activity of this novel LipHim1 gene encoded lipase in presence of Tween 60. Conventional hydrogen bonding with Leu135 and Arg137, carbon-hydrogen bonding with Pro71 and Asp139; alkyl and pi-alkyl interaction with Leu90 and Val99 and van der waal force of attraction with Phe132; Leu125; Gly78; Gly131; Val133; Ala79; Pro77; Ser75; Ala73; Leu94; Pro136 and Ala138 amino acid residues were revealed to be crucial role players. Keeping in view of potential applications of lipases, especially this novel reported LipHim1 gene encoded lipase in pharmaceutical industry, the knowledge gained from this study is expected to be critically important.