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Elucidation of lipase–substrate interactions will guide the proper industrial use and applicability of the enzyme. The aim of this study was to predict the 3 D structure of  Rhizopus oryzae  ZAC3 ( Ro ZAC3) lipase, study its interactions with some natural substrates and evaluate the feasibility of fatty acid methyl esters (FAME) production by the immobilized lipase. Protein identification of  Ro ZAC3 lipase was carried out using LC-MS/MS. The 3 D structure of the lipase was built using homology modelling and natural substrates such as tributyrin, tripalmitin and triolein were docked to the optimized 3 D model for investigation of enzyme-ligand interactions.  Ro ZAC3 lipase, immobilized by adsorption on Lewatit VP OC 1600 was applied in the synthesis of fatty acid methyl esters (FAME). From the phylogenetic analysis, it was observed that  Ro ZAC3 lipase was closely related (48%) to  Rhizopus javanicus  lipase (Q7M4U7). The predicted 3 D model was validated using the SWISS model validation server. Ramachandran and ERRAT plots were used to assess the amino acid environment and overall quality of the model. From the docking studies, the values of the binding energies obtained for tributyrin, tripalmitin and triolein were − 5.37, −5.27 and −5.77 respectively. At an enzyme:immobilization support ratio of 50 mg/g, transesterification reaction duration of 18 h and a temperature of 40 oC, the conversion reached above 80%. The molecular docking studies provided information on the interaction/modifications between the  Ro ZAC3 lipase and triacylglycerols that can be exploited for numerous applications. The immobilized lipase could serve in hydro-esterification reactions adaptable for biodiesel production. Communicated by Ramaswamy H. Sarma

journal of biomolecular structure and dynamics

Comparative modelling, molecular docking and immobilization studies on  Rhizopus oryzae  lipase: evaluation of potentials for fatty acid methyl esters synthesis