Multitarget Peptides Released by In Vitro Static Gastrointestinal Digestion of an Amaranth Protein Beverage.

Beverages formulated from alternative proteins, such as amaranth, are gaining attraction due to changes in human dietary patterns and environmental concerns like resource use and biodiversity loss. This study focuses on assessing the bioactive peptide release from an amaranth protein beverage. This beverage was subjected to a static simulated gastrointestinal digestion (SGD) protocol to evaluate its bioaccessibility and functional potential.

Characterization and Bile Acid Binding Capacity of Dietary Fiber Obtained from Three Different Amaranth Products.

Amaranth is a dicotyledonous plant, now considered a health-promoting food. It has been rediscovered by the worldwide food industry, which is increasingly becoming aware of the many uses and benefits provided by amaranth in various food preparations. Amaranth dietary fibers, soluble and insoluble fractions, obtained from flour, protein isolate, and beverage were physicochemically characterized and their potential bile acid binding capacity was evaluated.

Emulsifying Capacity of Cowpea Protein Isolates. Effect of Thermal and Hydrolytic Treatment.

In this work, modifications due to the effect of thermal treatments (TT 70 and 90 °C) and partial hydrolysis by digestion with alcalase (LH) on the emulsifying properties of cowpea protein isolates (CPIs) extracted at pH 8 and 10 were analyzed. In addition, the influence of protein concentration [0.1 and 1% (w/v)] was evaluated.

Spray-Dried Infant Formula Emulsion Stability as Affected by Pre-Heat Treatment and Total Solids Content of the Feed.

Pre-spray-drying processing may affect stability after reconstitution of emulsion-based powders, such as infant formulas. This study aimed to evaluate the effects of pasteurization temperature and total solids (TS) of the feed on the stability of the emulsions obtained from the reconstituted powders. Four infant formula powders (50%-75 °C, 50%-100 °C, 60%-75 °C, and 60%-100 °C) were produced at pilot scale, from emulsions with 50 or 60% TS pasteurized at 75 or 100 °C for 18 s.

Identification and characterization of antioxidant peptides obtained from the bioaccessible fraction of α-lactalbumin hydrolysate.

Whey is an abundantand sustainable source of bioactive peptides obtained from cheese making process. Whey proteins such as α-lactalbumin can be biologically active when the bioactive peptides encrypted in the amino acid sequence of the native protein are released by enzymatic hydrolysis. In the present work, the identification, sequence analysis, and antioxidant activity of bioaccessible peptides from α-lactalbumin alcalase-hydrolysate was assessed.