This study evaluated the antimicrobial activity (i.e., against Bacillus cereus and Staphylococcus aureus) and the antioxidant activity (i.e., ABTS, FRAP, and DPPH) of annatto seeds extract obtained by ultrasound-assisted extraction. A response surface design with three levels such as pH (2-11), solvent concentration (50-96 %), seed-to-solvent ratio (1:2–1:10), and treatment time (0-30 min) was employed to determine the optimal experimental conditions. Thus, a pH of 7.0, seed-to-solvent ratio of 1:7, and treatment time of 20 min were selected as optimal rendering an extract having a 0.62% of bixin, 3.81 mg gallic acid/mg equivalent of polyphenol compounds (ABTS 1035.7, FRAP 424.7, and DPPH 1161.5 μM trolox/L), and a minimal inhibitory concentration against Bacillus cereus and Staphylococcus aureus of 32 and 16 mg/L, respectively. Further, the main bioactive compounds identified by LC/ESI-MS were bixin and catechin, chlorogenic acid, chrysin, butein, hypolaetin, licochalcone A, and xanthohumol.
Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, milk proteins extracted from cows may cause food intolerance during infancy. Further, soybean, peanuts, tree nuts, fish, crustacean shellfish and egg proteins may act as antigens in 90% of children. Since the GI tract is permeable to intact antigens the oral intake of these proteins may generate gastrointestinal (50-80%), cutane ous (20-40%) and respiratory symptoms (4-25%). Most of these allergens are water-soluble glycoproteins that are resistant to acids and enzymes. Usually, these proteins have a small molecular weight (10,000-60,000 kDa), water solubility, glycosylation residues, and a rela tive resistance to heat and digestion. Allergenicity is less frequent in vegetable proteins due to their less flexible and non-compact structure. Allergenicity is also related to the resistance to proteolysis, post-translational glycosylation, presence of epitopes, and enzy matic proteolysis. Moreover, proteins serve as a coating material if structural modifica tions in the protein, either by physical, chemical or enzymatic mechanisms are conducted. As a result, their allergenicity is reduced, and their functional properties are enhanced.
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