dc.contributor | Universidade Federal da Bahia (UFBA) | |
dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.contributor | Univ Milan | |
dc.date.accessioned | 2021-06-26T06:17:39Z | |
dc.date.accessioned | 2022-12-19T23:08:54Z | |
dc.date.available | 2021-06-26T06:17:39Z | |
dc.date.available | 2022-12-19T23:08:54Z | |
dc.date.created | 2021-06-26T06:17:39Z | |
dc.date.issued | 2021-03-01 | |
dc.identifier | International Journal Of Molecular Sciences. Basel: Mdpi, v. 22, n. 6, 14 p., 2021. | |
dc.identifier | http://hdl.handle.net/11449/210774 | |
dc.identifier | 10.3390/ijms22063018 | |
dc.identifier | WOS:000645722200001 | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/5391376 | |
dc.description.abstract | Adzuki seed beta-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 beta-vignin isolate. Furthermore, the molecular features of the purified protein were investigated. The adzuki bean beta-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 beta-vignin protein, but also for a possible application as nutraceutical molecule. | |
dc.language | eng | |
dc.publisher | Mdpi | |
dc.relation | International Journal Of Molecular Sciences | |
dc.source | Web of Science | |
dc.subject | protein vicilin-type | |
dc.subject | protein fractionation | |
dc.subject | biological activities | |
dc.subject | in vitro digestibility | |
dc.subject | amino acid sequencing | |
dc.subject | glycosylated polypeptides | |
dc.subject | metal binding capacity | |
dc.title | Chromatography-Independent Fractionation and Newly Identified Molecular Features of the Adzuki Bean (Vigna angularis Willd.) beta-vignin Protein | |
dc.type | Artículos de revistas | |