Electrophoresis (SDS-PAGE) as a method for screening species of Passiflora using seed proteins as molecular markers.

• Main Author: STEPHAN, M. P.
• Publication Date: 2022
• Other Authors: COSTA, A. M., AZEVEDO, T. de L., ROSA, J. S. da, SANTOS, A. A. dos
• Format: Article
• Language: eng
• Source: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
• Download full: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1146660; https://doi.org/10.17265/2161-6264/2022.02.002
• topic: Bioactive peptides; P setacea; P tenuifila; Mass distribution on fruit; Tecnologia de Alimento; Método de Análise; Eletroforese; Purificação; Proteína; Peptídeo; Fruto; Maracujá; Semente; Casca; Polpa; Rastreamento; Food technology; Analytical methods; Polyacrylamide gel electrophoresis; Purification methods; Proteins; Peptides; Fruits; Passion fruits; Pulp; Passiflora; Seeds; Bioactive compounds

Brazil is the center of diversity and dispersion of species of the genus Passiflora. Two species of passion fruit Passiflora tenuifila BRS VT (passiflora garlic) and another of Passiflora setacea BRS PC were used in this study. The plants were grown on the Embrapa Cerrados experimental farm. The fruits were washed, minimally cut and their constituents separated. Both species differed in the proportion of wet mass between husk, seed, and pulp. As expected, both species had a higher proportion of husks and seeds and a lower amount of pulp. A semi-purification procedure for the proteins present in the seeds and husks was described and the molecular aspects were analyzed by polyacrylamide gel electrophoresis (SDS-PAGE). The quantification of soluble proteins was performed using the Bradford method. The analysis of the soluble protein extracted from the seeds and husks showed that these values are up to 70 times higher for the seeds of P. tenuifila and 28.5 times for P. setacea, in the husks. It was verified that both species present a similar protein profile, observed by the intense and diverse bands found in the polyacrylamide gel, mainly in the range of 32 to 19 kDa. This work opens up an unexplored field of tracking bioactive proteins and/or peptides including forms of nanostructure systems that protect other bioactive molecules. The objective of this work was to present an analytical procedure to semi-purify seed proteins of two Passiflora species and use electrophoresis as an analysis tool for further screening of their protein profiles and selection of a molecular marker to differentiate them.