National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
Lipase is one of the most imperative industrial enzymes and has a variety of applications in various industries. In the present study, lipases obtained by submerged cultivation of wild (LPF-5) and mutant (HN1) strain of A. niger were used and compared for characterization study. Activity and stability of partially purified lipase was determined under different pH, temperature, organic solvents and metal ions. The lipase showed highest activity and stability at pH 7.0 and temperature 35 °C for LPF-5 and 30 °C for HN1 strain. The lipases retained high activity over ranges of temperature (25-50 ºC) and pH (4.0-7.5). Lipase was enhanced by methanol and acetone, while slightly inhibited by butanol (10% v/v). Ca2+ appeared to be the excellent inducer of lipase activity. Lipase also showed stability in presence of the other metal ions (Na+, Ba2+, Mg2+, Cu2+, Fe2+ and Mn2+). The lipase of wild and mutant strain retained 10.58% and 14.60% of its activity when pre-incubated with Hg2+, indicating the inhibitory effect of Hg2+ on catalytic activity of lipase.
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