Insight into the structural configuration of metagenomically derived lipase from diverse extreme environment

Abstract The present study aims at finding the structural similarity of five metagenomically derived lipase protein sequences from diverse extreme environmental conditions i.e. hot springs, low-temperature regions, anaerobic lagoons and marine source. Using PROTPARAM server, the analysis of physicochemical characteristics of all lipases were found to be neutral in pH and are hydrophilic in nature except clone RK-Lip-479 and clone JKP01. The molecular weight varied from 31.2 kDa to 46.4 kDa while amino acid residues varied from 293 (clone FosC12) to 417 (clone JKP01). The instability index of all the proteins ranged from 22 to 35, which indicate their stability under given conditions except clone h1Lip1 lipase with higher instability index of 44.72 indicating less stable. Determination of the secondary structure of all proteins by SOPMA tool revealed the dominance of α-helices ranging between 27.34% (clone h1Lip1 lipase) to 45.05% (clone FosC12 lipase) and coils ranged between 27.3% (clone FosC12 lipase) to 34.53% (clone JKP01 lipase). 3D structures of all lipase proteins deduced using SWISS-MODEL automated server were found to be monomeric. The structures were retrieved and visualized using PyMol v0.99. The QMEAN values were within the range of 0.8 to 1.5 suggesting the models to be of suitable. The outcome of RAMPAGE and VERIFY3D servers for the models obtained were also observed to be of much suitable. The insight into the structural configurations of proteins revealed as above may help in varied applicability of metagenomics lipases.