Adzuki seed -vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure has been optimized and described. The electrophoretic analysis showed a high degree of homogeneity of -vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean -vignin was found to have a native size of 146 kDa, and the molecular weight determined was consistent with a trimeric structure. These were identified in two main polypeptide chains (masses of 56–54 kDa) that are glycosylated polypeptides with metal binding capacity, and one minor polypeptide chain with a mass 37 kDa, wherein these features are absent. The in vitro analysis showed a high degree of digestibility of the protein (92%) and potential anti-inflammatory capacity. The results lay the basis not only for further investigation of the health-promoting properties of the adzuki bean -vignin protein, but also for a possible application as nutraceutical molecule.

Chromatography-independent fractionation and newly identified molecular features of the Adzuki Bean (Vigna angularis Willd.) β-vignin protein / B. Philadelpho, V. Souza, F. Souza, J. Santos, F. Batista, M. Silva, J. Capraro, S. De Benedetti, G.C. Heinzl, E. Cilli, A. Scarafoni, C. Magni, E. Ferreira. - In: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. - ISSN 1661-6596. - 22:6(2021 Mar 16), pp. 3018.1-3018.14. [10.3390/ijms22063018]

Chromatography-independent fractionation and newly identified molecular features of the Adzuki Bean (Vigna angularis Willd.) β-vignin protein

J. Capraro;S. De Benedetti;G.C. Heinzl;A. Scarafoni;C. Magni
;
2021

Abstract

Adzuki seed -vignin, a vicilin-like globulin, has proven to exert various health-promoting biological activities, notably in cardiovascular health. A simple scalable enrichment procedure of this protein for further nutritional and functional studies is crucial. In this study, a simplified chromatography-independent protein fractionation procedure has been optimized and described. The electrophoretic analysis showed a high degree of homogeneity of -vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean -vignin was found to have a native size of 146 kDa, and the molecular weight determined was consistent with a trimeric structure. These were identified in two main polypeptide chains (masses of 56–54 kDa) that are glycosylated polypeptides with metal binding capacity, and one minor polypeptide chain with a mass 37 kDa, wherein these features are absent. The in vitro analysis showed a high degree of digestibility of the protein (92%) and potential anti-inflammatory capacity. The results lay the basis not only for further investigation of the health-promoting properties of the adzuki bean -vignin protein, but also for a possible application as nutraceutical molecule.
protein vicilin-type; protein fractionation; biological activities; in vitro digestibility; amino acid sequencing; glycosylated polypeptides; metal binding capacity
Settore BIO/10 - Biochimica
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/823626
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