Received: January 25, 2019;   Published: June 18, 2019

DOI: 10.32474/AOICS.2019.04.000181

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Abstract

Lipases are enzymes that catalyze the hydrolysis of long chain triglycerides. These enzymes have a key role in several human practices and industries, and it has been used in bioremediation processes. Due to the stability and specificity to their substrates under various conditions, their interest has grown during the last decade. The effluent from the palm oil industry contains about ~44% saturated fatty acids (mainly palmitic), ~37% monounsaturated fatty acids (mainly oleic acid) and 10% polyunsaturated fatty acids, potentially dangerous for the ecosystem. Bacteria and fungi contain lipases that are capable of degrade these lipids, but there are no sufficient studies on how these enzyme interacts with their substrates. In this study, by homology modeling, lipases 3D structure of Mucor circinelloides f. circinelloides 1006PhL and Rhizopus oryzae strains were modeled in silico using the SWISSMODEL server. The best models with stable structures were verified using the tool PROCHECK and Errat Server model. Further, a molecular docking was carried out between the selected modeled 3D structures with linoleic, linolenic, oleic, palmitic acid and tripalmitin using SwissDock tool to predict the lower binding energy of these lipases. Furthermore, the molecular docking analysis of 3D models of lipases from Mucor circinelloides f. circinelloides 1006PhL [EF405962] and Rhizopus oryzae [AER14043] suggest that pollutant fatty acids can bind to fungi lipases.

Keywords: Fatty acids; Fungi; Lipases; Homology modeling; Molecular docking

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Abstract| Introduction| Materials and Methods| Results and Discussion| Conclusion| References|