In silico CHARACTERIZATION OF LIPASE ARCHITECTURAL STRUCTURE IN Rhizobium leguminosarum

Lipases are the class of enzymes that hydrolyze the triglyceride and convert them to glycerol and fatty acids. This study provided the bioinformatics information about the Rhizobium leguminosarum Lipases. Physio-chemical properties were presented in details for different strains of Rhizobium leguminosarum. The total numbers of different strains of Rhizobium leguminosarum lipase’s residues were ranged from 504 (A0A072C2T8) to 208 (A0A072C300). Molecular Weight (MW) of different lipases were from 53657.02 (A0A072C2T8) to 22571.93 (A0A072C300). Rhizobium leguminosarum lipases are hydrophilic, soluble and cytoplasmic proteins. Numbers of Cys residues in different proteins were 3 to 5 however none of them forms the disulphide bond in the structure of lipases. The Isoelectric Points (pI) of the lipases were from 9.39 to 5.18 which represented the basic to acidic properties. Extinction coefficient (EC) of proteins were from 11460 (A0A072BXE4) to 46410 (A0A072C545) M-1.cm-1. The homology modelling of all 8 lipases were presented based on Swiss-model server. The evaluations of models were performed with PROCHECK program. These structures will provide valuable information for functional analysis of microbial lipases and can help in design the platform for engineering this enzyme.