Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense

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...

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Autores principales:	Abhijeet P. Herwade, Sainath S. Kasar, Niraj R. Rane, Shadab Ahmed, Jaswinder Singh Maras, Pankaj K. Pawar
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/530bdd12b1eb4e07a35bf17942bf0648
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spelling	oai:doaj.org-article:530bdd12b1eb4e07a35bf17942bf06482021-12-02T17:32:58ZCharacterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense10.1038/s41598-021-87980-82045-2322https://doaj.org/article/530bdd12b1eb4e07a35bf17942bf06482021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-87980-8https://doaj.org/toc/2045-2322Abstract 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 × 10−8 M) suggested strong inhibitory activity. Isothermal titration calorimetric analysis revealed its high affinity towards trypsin with dissociation constant (Kd) 2.28 µM.Abhijeet P. HerwadeSainath S. KasarNiraj R. RaneShadab AhmedJaswinder Singh MarasPankaj K. PawarNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Abhijeet P. Herwade Sainath S. Kasar Niraj R. Rane Shadab Ahmed Jaswinder Singh Maras Pankaj K. Pawar Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense
description	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 × 10−8 M) suggested strong inhibitory activity. Isothermal titration calorimetric analysis revealed its high affinity towards trypsin with dissociation constant (Kd) 2.28 µM.
format	article
author	Abhijeet P. Herwade Sainath S. Kasar Niraj R. Rane Shadab Ahmed Jaswinder Singh Maras Pankaj K. Pawar
author_facet	Abhijeet P. Herwade Sainath S. Kasar Niraj R. Rane Shadab Ahmed Jaswinder Singh Maras Pankaj K. Pawar
author_sort	Abhijeet P. Herwade
title	Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense
title_short	Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense
title_full	Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense
title_fullStr	Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense
title_full_unstemmed	Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense
title_sort	characterization of a bowman–birk type trypsin inhibitor purified from seeds of solanum surattense
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/530bdd12b1eb4e07a35bf17942bf0648
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Characterization of a Bowman–Birk type trypsin inhibitor purified from seeds of Solanum surattense

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