ISOLATION AND CHARACHTERIZATION OF CRUDE PROTEASE INHIBITORS FROM RICINUS COMMUNIS (Castor Beans)

Abstract

Protease inhibitors are frequently found in different sources such as animals, plants and
microorganisms and they inhibit the activity of proteases. In our studies protease
inhibitors (PIs) were isolated and characterized from plants tissues such as seeds. Ricinus
communis has shown highest inhibition activity as compared to other seeds (Glycin max,
Triticum astevium, Zey mays, Helianthus annus, Pennisetium typheides, Avena sativa,
Brassica compestris etc.) at optimized conditions. Crude protease inhibitor sample
(extracted from castor beans) incubated for 60 minutes at 35 ºC, using sodium phosphate
buffer pH =7.5, soluble casein as a substrate and trypsin enzyme were used for
maximum inhibition activity. The crude protease inhibitors were characterized at
different parameters such as effect of time period, substrate concentration, enzyme and
sample concentration, variable temperature and pH control.