Physicochemical Proprieties Of Lipase From Newly Streptomyces Sp. Olive Pomace Isolate

Résumé: Screening of new producing strains is required to meet the constant industrial demand for useful enzymes. In this context, an actinobacteria was isolated from the olive pomace, tested for extracellular lipase production, and identified by partial 16S rDNA sequencing. Then, the physicochemical characteristics of the enzyme are determined. Strain is a member of Streptomyces genus. Lipase was partially purified at 62.5 times, with a yield of 14.83% and a specific activity of 337.5 U/mg. Optimum activity was achieved at pH 7.0 and 60°C; it was completely preserved at pH 6.0 to 9.0, and more than 70% at 40 to 70°C, after 1 hour. The metal ions: K+, Na+, Ca2+, Co2+, Cu2+, Fe2+, Mg2+, Mn2+, and Zn2+ had no significant impact. Lipase activity was stable with ethylene diamine tetra acetic acid (EDTA), sodium dodecyl sulfate (SDS), H2O2, Triton x100, and Tween 80. Moreover, it was enhanced in butanol, chloroform, ethyl acetate, isopropanol, isobutyl acetate, hexane, petrol ether, and toluene. This enzyme can be suitable for various industrial applications.

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