Author:
Herwade Abhijeet P.,Kasar Sainath S.,Rane Niraj R.,Ahmed Shadab,Maras Jaswinder Singh,Pawar Pankaj K.
Abstract
AbstractA Bowman–Birk type trypsin inhibitor protein (SSTI) from seeds of the medicinal plant Solanum surattense was isolated, purified and characterized. SSTI showed a single band on SDS-PAGE corresponding to 11.4 kDa molecular weight. It is a glycoprotein (2.8% glycosylation) that differentially interacted with trypsin and chymotrypsin in a concentration-dependent manner. Its peptide sequence is similar to other Bowman–Birk type protease inhibitors found in Glycine max and Phaseolus acutifolius. The inhibitory activity was stable over a wide range of pH (1–10) and temperatures (10–100° C). Far-UV Circular Dichroism (CD) studies showed that SSTI contains β sheets (~ 23%) and α helix (~ 6%) and demonstrated structural stability at wide pH and high temperature. The kinetic analysis revealed a noncompetitive (mixed) type nature of SSTI and low inhibitor constant (Ki) values (16.6 × 10−8 M) suggested strong inhibitory activity. Isothermal titration calorimetric analysis revealed its high affinity towards trypsin with dissociation constant (Kd) 2.28 µM.
Funder
University Grants Commission
Department of Science and Technology, Government of India, New Delhi.
Dr. D. S. Kothari Postdoctoral Fellowship.
DST-FIST
Rajiv Gandhi Science and Technology Commission, Government of Maharashtra
Publisher
Springer Science and Business Media LLC
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