ArticleScientific reports2021
Characterization of a Bowman-Birk type trypsin inhibitor purified from seeds of Solanum surattense.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Evolution, structural diversity and functional plasticity of plant derived multifunctional proteases and α-amylases inhibitors.Plant molecular biology · 2026Review
- Accelerating the coagulation of germinated soymilk by glucono-δ-lactone using different physical treatments and quality assessment of separated soybean whey.Food chemistry: X · 2026Article
- Pleiotropic effects of recombinant protease inhibitors in plants.Frontiers in plant science · 2022Review
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Authors and funding
6 authors.
Funding
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Abstract
A 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
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