HEAT STABILITY AND PROTEASE INHIBITORY PROPERTIES OF 28KDa GLYCOPROTEIN FROM TURMERIC (CURCUMA LONGA)
Dinesha Ramadas, Shobith Rangappa, Santhosh Kumar N.*, Chikkanna D., Manjula R. V., Tejaswini B.M, Divya Y.
Turmeric (Curcuma longa) belongs to Zingiberaceae family extensively used as food colourant, flavour, spice and as medicine in Middle Asia and South East Asian countries. Herein we are reporting the property of heat stability and proteases like trypsin and chymotrypsin inhibitory property of glycoprotein of 28kDa from Curcuma longa. It exerts inhibitory activity protease Trypsin and Chymotrypsin up to 53 and 57% at 100μM dosage respectively. The protein alone shows 67% inhibition and standard antioxidant Ascorbic acid shows 65%. This protein was stable up to a temperature of 1000C, active over a wide range of pH from 2 to 12, specifically more at weak acidic and neutral pH and less at basic pH. This is the first report on protease inhibitor activity and heat stability activity of glycoprotein of 28kDa from Turmeric (Curcuma longa).
Keywords: Turmeric, Curcuma longa, Heat stability, Protease inhibitors, trypsin and chymotrypsin.
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