Abstract
This study purified and characterized lipases secreted by a fungus Mucor jansenii isolated from the effluent of a cocoa processing plant. This was done in an effort to investigate the fungus' ability to produce lipase for industrial and biotechnological uses. The fungus isolated was identified macroscopically and microscopically using Lactophenol cotton blue stain. The enzyme produced was purified partly by ion-exchange chromatography on QAE-Sephadex A-25. Specific activity of the partially purified Mucor jansenii B6 lipase was 680.33 units/mg protein, 350.11 units/mg protein, and 342.19 units/mg protein, respectively, for isoforms A, B, and C. Partly purified M. jansenii B6 lipase had a molecular weight of 127 kDa, as determined by gel fitment on the Sephacryl S-200 column. The optimum pH and temperature for enzyme activity were 11.0 and 50 oC, respectively. The enzyme activity was enhanced by Ba2+, Na+, Ca2+, and Mg2+ at 5 mM and 10 mM, while Al3+ reduced the catalytic activity. Activity of the enzyme increased in acetone but decreased in ethyl acetate. The Michaelis constant (Km) and maximum velocity (Vmax) of the enzyme were found to be 0.5 mM and 16.6 units/mg protein, respectively. The study concluded that Mucor jansenii B6 lipase is a potential alkaline and thermostable lipase suitable for industrial and biotechnological applications.
Published Version
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