The objective of this study was to investigate the impact of 24‐ and 48‐h germination on antinutrient levels (phytic acid, trypsin inhibitors, saponins, and tannins), in vitro starch and protein digestibility, and the content and bioaccessibility of phenolic compounds and antioxidants in chickpeas, peas, mung beans, and lentils. Germination resulted in reductions of phytic acid by up to 75.65% and trypsin inhibitor activity by up to 39.20% in the pulses studied. In contrast, saponin levels showed a significant increase, rising nearly threefold with germination, while mung beans exhibited an exceptional 27‐fold increase. Tannins decreased in lentils (2.6‐fold) and mung beans (5.8‐fold), increased in peas (1.6‐fold), and remained unchanged in chickpeas following germination. In vitro protein digestibility generally increased with germination, reaching up to 4.40%, except in peas, where a decline was observed. Germination significantly enhanced total digestible starch content while reducing resistant starch in all pulses except chickpeas. Mung beans exhibited the highest total phenolic content and antioxidant capacity, followed by lentils. Although germination significantly elevated total phenolic content in all pulses, this increase did not always align with antioxidant capacity outcomes. Additionally, germination led to a decline in the bioaccessibility of phenolics. However, the amount of phenolic compounds progressively increased during gastric and intestinal digestion, with intestinal digestion further enhancing the total antioxidant capacity of the pulses.

This study aimed to investigate the effect of enzymatic hydrolysis on the physicochemical, functional, and antioxidant properties of safflower protein isolate and hydrolysates. Isolated safflower protein was hydrolyzed by both Alcalase and Flavourzyme at the degree of hydrolysis of 2%, 4%, 6%, 8%, and 10%. Safflower protein hydrolysates exhibited a lighter color (3.74%–8.79%) and reduced redness (69.11%–102.85%) with lower cohesiveness (15.29%–21.76%) and better flowability (25.91%–40.27%) compared to the protein isolate. Moreover, the surface hydrophobicity of safflower protein isolate decreased up to 73.18% with hydrolysis, while solubility increased up to 54.42% at pH 4–7. Safflower proteins hydrolyzed with Alcalase had higher oil binding, foaming, and emulsion capacities than samples hydrolyzed with Flavourzyme, while their water holding capacities were lower. Furthermore, safflower proteins hydrolyzed with Alcalase at an 8% degree of hydrolysis displayed the highest foaming capacity (up to 3.89 times) and emulsion capacity (up to 1.23 times) in all samples. However, it had poor foam (up to 67.06%) and emulsion stability (up to 74.35%). Additionally, safflower protein hydrolysates demonstrated higher ABTS^•+ and DPPH radical scavenging activity. Overall, safflower protein hydrolysates showed better physicochemical, functional, and antioxidant properties than protein isolates, depending on enzyme types and degree of hydrolysis.

In this study, the effects of the drying method and spray drying inlet air temperature on the color, surface morphology, hydrophobicity, powder and functional properties of safflower protein isolate were investigated. Safflower protein was extracted using the alkaline extraction and isoelectric precipitation method and then dried using freeze-drying and spray-drying at 140, 150, 160, 170, and 180 ^°C inlet air temperatures. When compared to the spray-dried samples, freeze-dried safflower protein isolate had lower cohesiveness (1.18) and better flowability (15.12%) with higher bulk density (0.31 g/cm³) and lower tapped bulk density (0.37 g/cm³). Additionally, its wetting time (9.00 s) was also found to be lower. On the other hand, spray-dried samples exhibited lighter color, higher foaming capacity (30.00–38.75%) and stability (87.50–89.17%), and emulsion activity (51.25–54.50%) and stability (85.76–87.51%) than the freeze-dried sample. Moreover, it was found that the foaming capacity and emulsion activity of safflower protein spray-dried at 140 ^°C were higher than those of other spray-dried samples. Overall, freeze-dried safflower protein showed better powder properties, while spray-dried samples had better functional properties. Consequently, it was shown that the choice of drying method and spray drying inlet air temperature were critical for the powder and functional properties of safflower protein.