Abstract

PARTIAL PURIFICATION AND CHARACTERISATION OF LIPASE FROM EUPATORIUM ODORATUM

Deepa G. Muricken* and Neethu K. R.

ABSTRACT

Eupatorium odoratum belongs to asteraceae family and this plant in grown widely in tropical climates. The present study utilizes this plant as a source of lipase enzyme which has wide range of applications in the food, detergent, and pharmaceutical sectors. Lipase enzyme is a naturally occurring enzyme found in the stomach and pancreatic juice. They function is to digests fats and lipids, helping to maintain correct gall bladder function. The rich foliage from this plant can be utilized as the enzyme source. Lipase was extracted from Eupatorium odoratum leaf and purified partially using ammonium sulphate precipitation, dialysis and ion exchange chromatography on DEAE cellulose column. The purified enzyme was characterized for its size, optimum temperature, pH and thermal stability. The purified enzyme had a specific activity of 0.0599 meq/min/g. The molecular weight was found to be 66 kDa as determined by SDS- PAGE. Enzyme showed a maximum activity at 60°C and at pH 7.0. Enzyme retained its 66.67% activity after two and half hours of incubation at 70°C.

Keywords: lipase, Eupatorium odoratum, molecular weight, thermal stability, optimum temperature, pH.