Antinutrients (ANs) interact with proteins changing its behavior and may affect Maillard reaction (MR). This work aimed to study the effect of phytic acid, tannic acid, and saponin on asparagine-glucose MR. The effect of AN concentration (0-1 mM) and reaction time (3-30 min at 150 °C) on the formation of melanoidins and acrylamide was determined.
View Article and Find Full Text PDFPlant-derived protein can present antinutrients (ANs) in its composition. The ANs can interact with the protein, affecting its solubility and functional properties, such as gelation. This work evaluated the effect of three ANs, namely phytic acid (PA), tannic acid (TA), and Quillaja bark saponin (QBS), on the gelation and solubility of soy (SPI), pea (PPI), and rice protein isolate (RPI).
View Article and Find Full Text PDFSaponins are known for their bioactive and surfactant properties, showing applicability to the food, cosmetic and pharmaceutical industries. This work evaluated the saponins effects on Kluyveromyces lactis β-galactosidase activity and correlated these changes to the protein structure. Enzyme kinetic was evaluated by catalytic assay, protein structure was studied by circular dichroism and fluorescence, and isothermal titration calorimetry was used to evaluate the interactions forces.
View Article and Find Full Text PDFTannins, proteins, and divalent cations interactions are important for many processes in the food industry and human and animal nutrition and health. The effect of magnesium, calcium, and manganese on the interaction, turbidity, and in vitro protein digestibility of bovine serum albumin and tannic acid complexes was studied. The divalent cations increase the affinity and influence the enthalpy and entropy changes of the protein and tannin binding.
View Article and Find Full Text PDFTannins are compounds with antinutrient properties that hinder food digestibility, prejudicing human and animal nutrition. This work aimed to evaluate the negative effects of tannic acid on Kluyveromyces lactis β-galactosidase catalytic activity and correlate these changes with the protein structure. β-Galactosidase activity decreased in the presence of tannins, which caused changes to the structure of the enzyme, as demonstrated by circular dichroism.
View Article and Find Full Text PDFPhytate decreases mineral and protein availability and influences protein properties, such as solubility and stability. The binding constants and turbidity data can help with the understanding of the influence of phytate and divalent salts on protein behavior. Ternary complexes formed between bovine serum albumin, sodium phytate, and divalent salts were investigated by isothermal titration calorimetry, turbidity, and in vitro protein digestibility.
View Article and Find Full Text PDFBioavailability of food nutrients can be reduced in the presence of antinutrients such as phytates and tannins. This work aimed to study bovine serum albumin binding to phytic acid and tannic acid, and its influence on in vitro protein digestibility. The effect of autoclaving and boiling on protein digestibility and the microstructure of complexes was also evaluated.
View Article and Find Full Text PDFThis work aimed to study the influence of pH (3.5 and 7.0) and CaCl and MgCl addition on heat-set gelation of a quinoa protein isolate at 10% and 15% (w/w).
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