Biochemical Characterization of Extracellular Lipase from an Improved Strain of Penicillium Citrinum KU613360

Abstract

In the present study lipase purified from an improved strain of Penicillium citrinum KU613360 was subjected to biochemical characterization. The lipase showed maximum activity at optimum pH of 6.5 andtemperature 40°C respectively.It wasobserved that lipase showed specificity for long chain fatty acids (Triolein (C18;1) and Trilinoclenin (C18; 3)) than short chain fatty acids.The metal ion stability studies indicate that the lipase activity was maximum with Mn2+, Ca2+, Mg2+(1mM and 10mM)and the lipase activity is inhibited by Hg and Zn.The kinetic parameters of improved strain ofP.citrinumwere also evaluated and the recorded value of Km was found to be 19.33±0.010mM and Vmax was 83.33±0.06 (μmole min-1mg-1) respectively. Thus, from our results it was concluded that the improved strain has considerable capability and potentiality for the industrial applications.