%0 Journal Article
%T Studies on Properties of Lipase Produced from <i>Aspergillus</i> sp. Isolated from Compost Soil
%A Chijioke O. Ezenwelu
%A Oladejo A. Afeez
%A Obiano U. Anthony
%A Okoro A. Promise
%A Ude-Ezika C. Mmesoma
%A Oparaji E. Henry
%J Advances in Enzyme Research
%P 49-60
%@ 2328-4854
%D 2022
%I Scientific Research Publishing
%R 10.4236/aer.2022.102003
%X Lipase producing <i>Aspergillus </i>was isolated from soil collected from a refuse dump site located at Awka,
Anambra State, Nigeria using standard microbiology and biochemical techniques.
Crude extract of lipase was produced after a successful screening of the
isolates using mineral broth containing p-NPP through submerged fermentation
system with optimized physiologic conditions<i>. </i>Three steps of purification were carried out: Ammonium sulphate, dialysis
and gel filtration (sephadex G-150). Crude extract was precipitated by using
70% saturation of ammonium sulphate at pH 6.0 which gave the optimum precipitation
of the protein with specific activity of 260.56 U/mg. Precipitation using
ammonium sulphate carried out at pH 6.5 and 8.0 gave specific activity of 217
U/mg of the protein. The precipitates were further desalted through dialysis
for twelve hours and specific activity of 343.20 U/mg was recorded from the
dialysate afterwards. Further purification was done by using sephadex G-150 and
specific activity of 490.55 U/mg was recorded from the active pooled fractions.
The purification table showed a 2.32 purification folds of lipase was gotten
after gel filtration (sephadex G-150) with a lipase percentage yield of 2.00%.
The specific activity of lipase increased from 211.81 to 490.55 U/mg.
Characterization of <i>¦Â</i>-galactosidase
gave optima pH and temperature of the enzyme at 6.0 and 60¡ãC respectively.
Kinetic constants: K<sub>m</sub> and V<sub>max</sub> values were obtained at
various concentrations of p-NPP where 0.32 mM and V<sub>max</sub> of 200.00 ¦Ìmol/min
respectively. Ca<sup>2+</sup> and Co<sup>2+</sup> showed greater effect on lipase
activity in a concentration-dependent manner (0.03 - 0.05 M) when compared to
Mn<sup>2+</sup> and Fe<sup>2+</sup>. The results from this study have shown
that lipase produced from filamentous <i>Aspergillus </i>has a wide range of activity over physiologic conditions in regards to
industrial and clinical standard operational procedures.
%K Lipase
%K Purification
%K Specific Activity
%K Precipitation
%K Purification Folds
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=117829