We developed a protein-enriched umbu (S. tuberosa) jam by adding Spirulina sp. LEB-18 to it to improve its nutritional value. Three formulations were developed: UJ1 (jam without Spirulina), UJ2spirulina (jam with 1.0% Spirulina), and UJ3spirulina (jam with 1.4% Spirulina). Physicochemical properties, chemical composition, and sensory acceptance were determined. Jam products were deemed to be stable and safe for consumption because their water activity (Aw; 0.58-0.61), pH (2.60-3.42), and total titratable acidity (14.59-22.27%) values were considered to prevent the growth of microorganisms. There were statistically significant differences in these parameters, except for the Aw, among the umbu jams with Spirulina. The moisture content was lower in the jams produced (10.66-16.79%) than in commercial formulations, but the energy value (332.91-358.87 kcal/100 g) was higher when compared to other studies. In this study, the most significant result was that the supplementation of umbu jam with 1.0% and 1.4% of Spirulina statistically significantly increased the amount of protein (136-232%) and total ash (96-235%). Furthermore, the acceptability indices for UJ1, UJ2spirulina, and UJ3spirulina were 81.3, 78.0, and 75.3%, respectively, and therefore, they were considered as acceptable products (over 70%). Thus, the results indicate that supplementation with Spirulina sp. LEB-18 may improve the nutritional value of food and provide health benefits when incorporated into different food industry products, especially as a protein-enriched functional food ingredient.
In this study, in silico approaches are employed to investigate the binding mechanism of peptides derived from cowpea β-vignin and HMG-CoA reductase. With the obtained information, we designed synthetic peptides to evaluate their in vitro enzyme inhibitory activity. In vitro, the total protein extract and <3 kDa fraction, at 5000 µg, support this hypothesis (95% and 90% inhibition of HMG-CoA reductase, respectively). Ile-Ala-Phe, Gln-Gly-Phe, and Gln-Asp-Phe peptides were predicted to bind to the substrate binding site of HMGCR via HMG-CoAR. In silico, it was established that the mechanism of HMG-CoA reductase inhibition largely entailed mimicking the interactions of the decalin ring of simvastatin and via H-bonding; in vitro studies corroborated the predictions, whereby the HMG-CoA reductase activity was decreased by 69%, 77%, and 78%, respectively. Our results suggest that Ile-Ala-Phe, Gln-Gly-Phe, and Gln-Asp-Phe peptides derived from cowpea β-vignin have the potential to lower cholesterol synthesis through a statin-like regulation mechanism.
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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