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New Molecular Features of Cowpea Bean (Vigna Unguiculata, L. Walp) Β-Vignin

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New Molecular Features of Cowpea Bean (Vigna Unguiculata, L. Walp) Β-Vignin Bioscience, Biotechnology, and Biochemistry ISSN: 0916-8451 (Print) 1347-6947 (Online) Journal homepage: https://www.tandfonline.com/loi/tbbb20 New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin Ederlan de Souza Ferreira, Jessica Capraro, Fabio Sessa, Chiara Magni, Aureluce Demonte, Alessandro Consonni, Valdir Augusto Neves, Eduardo Maffud Cilli, Marcello Duranti & Alessio Scarafoni To cite this article: Ederlan de Souza Ferreira, Jessica Capraro, Fabio Sessa, Chiara Magni, Aureluce Demonte, Alessandro Consonni, Valdir Augusto Neves, Eduardo Maffud Cilli, Marcello Duranti & Alessio Scarafoni (2018) New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin, Bioscience, Biotechnology, and Biochemistry, 82:2, 285-291, DOI: 10.1080/09168451.2017.1419855 To link to this article: https://doi.org/10.1080/09168451.2017.1419855 View supplementary material Published online: 17 Jan 2018. Submit your article to this journal Article views: 111 View Crossmark data Full Terms & Conditions of access and use can be found at https://www.tandfonline.com/action/journalInformation?journalCode=tbbb20 BIOSCIENCE, BIOTECHNOLOGY, AND BIOCHEMISTRY, 2018 VOL. 82, NO. 2, 285–291 https://doi.org/10.1080/09168451.2017.1419855 New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin Ederlan de Souza Ferreiraa, Jessica Caprarob, Fabio Sessab, Chiara Magnib, Aureluce Demontec, Alessandro Consonnib, Valdir Augusto Nevesc, Eduardo Maffud Cillid, Marcello Durantib and Alessio Scarafonib aDepartment of Bromatological Analysis, School of Pharmacy, Federal University of Bahia, Salvador, Brazil; bDepartment of Food, Environmental and Nutritional Sciences (DeFENS), Università degli Studi di Milano, Milan, Italy; cDepartment of Food and Nutrition, São Paulo State University, Araraquara, Brazil; dChemistry Institute, Sao Paulo State University, Araraquara, Brazil ABSTRACT ARTICLE HISTORY Cowpea seed β-vignin, a vicilin-like globulin, proved to exert various health favourable Received 28 September 2017 effects, including blood cholesterol reduction in animal models. The need of a simple scalable Accepted 8 December 2017 enrichment procedure for further studies for tailored applications of this seed protein is crucial. KEYWORDS A chromatography-independent fractionation method allowing to obtain a protein preparation Vigna ssp; vicilin proteins; with a high degree of homogeneity was used. Further purification was pursued to deep the β-vignin; glycosylation; metal molecular characterisation of β-vignin. The results showed: (i) differing glycosylation patterns of ion binding the two constituent polypeptides, in agreement with amino acid sequence features; (ii) the seed accumulation of a gene product never identified before; (iii) metal binding capacity of native protein, a property observed only in few other legume seed vicilins. The nutritional relevance of grain legumes primarily and particularly in North Eastern Brazil [5]. Despite the relies upon their high contents of protein, which vary rich protein content of cowpea (210 g to 340 g/kg) and a from 200 to 300 g/kg in peas and beans up to 380–400 g/ high concentration of calcium, potassium, iron, zinc and kg in soybean and lupin. Legume proteins are gaining copper [5], as well as a number of positive agronomic interest as ingredients in food systems too, especially features, including drought resistance and adaptation to in the industrialized countries, where a growth in per poor soils, Vigna seeds are not widely consumed yet. The capita consumption of grains has been observed [1]. incomplete appreciation of the molecular, technological, According to Alonso et al. [2], a number of desirable nutritional and nutraceutical properties of Vigna seed features of legume proteins, which affect both the qual- components is one of the reasons of this limitation [6]. ity and behaviour of proteins in food systems during As for most legume seeds, the main protein frac- processing, manufacturing, storage and preparation, are tion of cowpea seeds is represented by globulins which required for their optimal food utilisation. In turn, the accounts for 51 to 72% of total seed proteins. The most search for novel seed protein sources stimulates research represented protein type is β-vignin, which belongs to studies aiming at the characterisation and improved the 7S globulin or vicilin-like family [7–10]. The 7S glob- isolation of proteins from under-utilized legumes. ulins of Vigna species show 62% amino acid sequence Furthermore, health-promoting biological activities and identity with soybean β-conglycinin α’ subunit, which regulatory functions in human body have been related proved to be effective in lowering blood cholesterol and to several protein components of plant origin in recent triglycerides levels in humans and animals [11–14]. years. Plant peptides of different sizes and even intact Indeed, recent results by our research groups have shown proteins were shown to exert various beneficial effects a specific hypocholesterolaemic effect of rat-adminis- in humans, notably in bone and cardiovascular health, tered oral doses of β-vignin isolated from cowpea [15]. inflammation, cancer, weight control, insulin sensitivity Other authors observed that the hydrolysis product of and immune-cell activity [3]. total protein extract from cowpea favourably affects lipid Cowpea (Vigna unguiculata, L. Walp) seeds are metabolism, through the inhibition of cholesterol syn- among the most relevant Vigna species for human thesis [16]. food. Cowpea bean is cultivated and primarily con- The study of cowpea β-vignin molecular properties sumed as a food in tropical and subtropical zones of has already been approached by few authors [8,17]. the world, including Africa, Asia and Latin America [4] The techno-functional results are reported by Horax CONTACT Jessica Capraro [email protected] Supplemental data for this article can be accessed 10.1080/09168451.2017.1419855. © 2018 Japan Society for Bioscience, Biotechnology, and Agrochemistry .E. DE SOUZA FERREIRA ET AL 286 et al. [18] and Zhang et al. [19]. However, improved or P11827_SOYBN and the sequence of lupin 7S globu- simplified protocols for protein fractionation, as well lin was UniProtKB: Q53HY0_LUPAL. The sequences as the full characterisation and evaluation of the nutri- were aligned by Clustal O and Lalign at https://www. tional and nutraceutical properties of this protein are expasy.org; prediction of N-glycosylation was carried still scarcely investigated. In this work, we describe a out by Net-N-Glyc 1.0 Server at http://www.cbs.dtu. simplified procedure, which allowed the preparation of dk/services/NetNGlyc/; Protein Parameters at https:// highly purified β-vignin from cowpea seed. Moreover, www.expasy.org was used to calculate theoretical pI and its further molecular characterisation led us to identify molecular mass of the polypeptide chains. novel molecular features such as the glycosylation pat- tern and metal binding capacity. Extraction and isolation of raw β-vignin from cowpea seeds Material and methods Cowpea seeds were first imbibed in distilled water for Plant material and chemicals 10 h. Subsequently, the hull was removed manually. The seeds were then placed in an oven with air circulation at Cowpea (V. unguiculata, L. Walp) seeds were kindly 40 °C for 12 h. Then, the seeds were milled to a flour and provided by Dr. Rogério Faria Vieira of the Centro sieved through a 60 mesh nylon filter. The flour obtained Tecnológico da Zona da Mata da Empresa de Pesquisa was not defatted. Agropecuária de Minas Gerais (Viçosa, MG, Brazil). All The whole procedure is schematically shown in Figure chemicals were from Sigma-Aldrich® (Milan, Italy), if 1. The procedure consisted in the extraction of the flour not otherwise stated. with 0.1 M NaCl solution in the ratio 1/20 (w/v), adjusted to pH 7.5 with 2 M NaOH. Stirring was applied at room Structural homology by bioinformatic analyses temperature for 1 h. The suspension was then filtered The available sequences of cowpea β-vignin were through a nylon filter as above and then centrifuged at obtained from NCBI and UniProtKB. The following 10,000 g for 40 min at the same temperature. From this entries were used: NCBI Blast: AM905848; UniProtKB: step on, all procedures were carried out at 4 °C. The A8YQH5_VIGUN for 7S-cowpea. All sequences are clas- supernatant was diluted 1/1 with distilled water; pH was sified as “fragment”. The sequences of 7S-adzuki globulin adjusted to 5.0 with 2 M HCl and the solution was kept by UniProtKB: A4PI98_PHAAN; soybean β-congly- overnight at 4 °C. A further centrifugation step as above cinin subunit was that of the α′ subunit UniProtKB: allowed obtaining a soluble fraction (albumins) and a Figure 1. Large scale, chromatography-independent isolation of the β-vignin from cowpea flour. BIOSCIENCE, BIOTECHNOLOGY, AND BIOCHEMISTRY 287 pellet. The pellet was suspended in water 1:20 w(ini- SDS–PAGE tial weight)/v and stirred at 4 °C for 10 min. Then, the One-dimensional gel electrophoresis in the presence pH was adjusted to 5.0 and the suspension centrifuged of 2% 2-mercaptoethanol was performed on 12% pol- as above. The new pellet was dissolved in 0.1 M NaCl, yacrylamide gels, using a Mini Protean II cell (Bio- 1:10 w(initial weight)/v at pH 7.0 and stirred at 4 °C for Rad, Hercules, CA, USA) according to Laemmli [21]. 20 min. After further centrifugation as above, the pellet Marker proteins of known molecular weight were used was discarded and
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