Chromatography-Independent Fractionation and Newly Identified Molecular Features of the Adzuki Bean (Vigna angularis Willd.) β-vignin Protein |
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| Authors: | Biane Philadelpho Victria Souza Fabiani Souza Johnnie Santos Fabiana Batista Mariana Silva Jessica Capraro Stefano De Benedetti Giuditta C Heinzl Eduardo Cilli Alessio Scarafoni Chiara Magni Ederlan Ferreira |
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| Affiliation: | 1.Department of Bromatological Analysis, School of Pharmacy, Federal University of Bahia, 40170-115 Salvador, Brazil; (B.P.); (V.S.); (F.S.); (J.S.); (F.B.);2.Chemistry Institute, Sao Paulo State University, 14800-900 Araraquara, Brazil; (M.S.); (E.C.);3.Department of Food, Environmental and Nutritional Sciences (DeFENS), Università degli Studi di Milano, 20133 Milan, Italy; (J.C.); (S.D.B.); (G.C.H.); (A.S.) |
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| Abstract: | Adzuki seed β-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 β-vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean β-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 β-vignin protein, but also for a possible application as nutraceutical molecule. |
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| Keywords: | protein vicilin-type protein fractionation biological activities in vitro digestibility amino acid sequencing glycosylated polypeptides metal binding capacity |
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