In this study, three samples of olive oil wastes: Olive Rinse Water (OR), Olive Mill Wastewater (OM) and Olive Pomace (OP), which were collected from an olive oil mill located at Fez-Morocco, were analyzed for their microbiota. A total of 81 isolates were obtained and constituted a microbial bank formed of 35 bacteria, 41 yeasts and 5 fungi. The microbial communities have been compared in term of metabolic potential by testing hydrolytic enzymes activities of lipase, protease, amylase, cellulase, pectinase and tannase on agar plate media. The results reveal that among the examined microorganisms, 68 isolates were able to produce at least one of the screened enzymes. The pectinase activity was the predominant one (39.51%), followed by cellulase activity (34.57%) and by lipase activity (27.16%). However, the amylase activity was observed only for 11.11% of the studied isolates, followed by protease activity (9.88%) and by tannase activity 6.17%. Thereby, considering the isolates ability to produce enzymes, they can be considered as potential candidates for industrial and biotechnological applications. Lipases
A newly isolated strain, Proteus vulgaris OR34, from olive mill waste was found to secrete an alkaline extracellular lipase at 11 U• ml -1 when cultivated on an optimized liquid medium. This lipase was purified 94.64fold with a total yield of 9.11% and its maximal specific activity was shown to be 3232.58 and 1777.92 U•mg -1 when evaluated using the pH-stat technique at 55℃ and pH 9 and Tributyrin TC4 or olive oil as the substrate. The molecular mass of the pure OR34 lipase was estimated to be around 31 kDa, as revealed by SDS-PAGE and its substrate specificity was investigated using a variety of triglycerides. This assay revealed that OR34 lipase preferred short and medium chain fatty acids. In addition, this lipase was stable in the presence of high concentrations of bile salt (NaDC) and calcium ions appear not to be necessary for its activity. This lipase was inhibited by THL (Orlistat) which confirmed its identity as a serine enzyme. In addition, the immobilization of OR34 lipase by adsorption onto calcium carbonate increased its stability at higher temperatures and within a larger pH range. The immobilized lipase exhibited a high tolerance to organic solvents and retained 60% of its activity after 10 months of storage at 4℃. Finally, the OR34 lipase was applied in biodiesel synthesis via oleic acid mediated esterification of methanol when using hexane as solvent. The best conversion yield (67%) was obtained at 12 h and 40℃ using the immobilized enzyme and this enzyme could be reused for six cycles with the same efficiency.
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