Production of lipase in a fermentor using a mutant strain of <i>Corynebacterium </i>species: Its partial purification and immobilization

Abstract

Extracellular <i>Corynebacterium </i>lipase was produced using a 2.5 L Chemap ferrnentor using 1300 ml fermentation medium at temperature 33°C, agitator speed 50 rpm, aeration rate 1 VVM having K_La 16.21hr^-l. Crude lipase was purified by salting out method followed by dialysis and immobilized using calcium alginate gel matrix followed by glutaraldehyde

cross linking Purification process increased specific activity of enzyme from 2.76 to 114.7 IU/mg<i>. </i>Activity of immobilized enzyme was 107.31IU/mg. Optimum temperature for purified and immobilized enzyme activity were 65° and 50°C respectively. Optimum <i>p</i>H<i> </i>was 8.0 in both the cases, K_m and V_max value for purified lipase were 111.1 μmol/min and 14.7% respectively. Ca²⁺ (5 m<i>M</i>) was found to be stimulator for enzyme activity. Immobilized lipase retained 68.18% of the original activity when stored for 40 days.