Brewers spent grain protein hydrolysate as a functional ingredient for muffins: antioxidant, antidiabetic, and sensory evaluation

This study assessed the fortification of muffins with 2, 4, and 6 % of brewer's spent grain protein hydrolysates to enhance their in vitro antioxidant, α-glucosidase, and α-amylase inhibitory activities. In addition, oxidative stability, hardness, color and sensory properties of fortified muffins were investigated. The fortification of muffin formulations with 6 % hydrolysates increased antioxidant activity six times higher than that of the control sample. As the hydrolysate increased to 6 %, the α-amylase and α-glucosidase inhibition also increased to 88 and 40 %, respectively. The 6 % fortified muffins exhibited lower peroxide and thiobarbituric acid values during a 14 day storage than the control muffins, while higher hydrolysate levels darkened the color and softened the texture. Sensory evaluation indicated that muffins with 2% hydrolysates achieved similar overall acceptance as the control. It can be concluded that brewer's spent grain hydrolysate is suitable for functional bakery products.Universidade de Vigo/CISU

Potential inhibitory effect of fish, maize, and whey protein hydrolysates on advanced glycation end‐products (AGEs)

Abstract Advanced glycation end‐products (AGEs) are produced in the final stage of the Maillard reaction. AGEs formation may be inhibited by natural hydrolysates derived from plant or animal sources. The present study aimed to investigate the antiglycation potential of fish, maize, and whey protein hydrolysates. It was carried out in four model systems, Bovine serum albumin (BSA)‐Glucose, BSA‐Fructose, BSA‐Sorbitol, and BSA‐HFCS (high fructose corn syrup), by evaluation of fluorescent intensity of AGEs after seven days of reaction at 37°C. The results showed that the highest inhibitory effect belonged to 0.16% of FPH (fish protein hydrolysate, percent inhibition ~99.0%), whereas maize protein hydrolysate (MPH) had lower antiglycation activity in comparison with FPH. Among all hydrolysates, whey protein hydrolysate with the lowest degree of hydrolysis showed the weakest inhibitory activity. Overall, our results indicated that the investigated hydrolysates, particularly FPH, have promising antiglycation potential and can be recommended for the production of functional foods

Interconnections of primary and secondary metabolites of Astragalus verus cells under selenium treatment

Selenium (Se) is a beneficial microelement with dose dependent effects on plants. At low concentrations, it stimulates antioxidant system but at high doses cause cell death. In the present study, the effects of different concentrations of Se (0, 0.5, 2.5, 12.5, and 62.5 μM) on metabolome of a cell line of Astragalus verus was evaluated. Seven-old days cells were treated with Se in the middle of their logarithmic growth phase for one week. Along with the increasing concentrations of Se, growth and total contents of soluble sugars and proteins, auxin and brassinosteroid decreased. However, the contents of ascorbate, glutathione, certain phenolics, free amino acids, and the activity of antioxidant enzymes increased. The results indicated the signaling role of monosaccharides and their synergistic behavior with auxin and brassinosteroid and critical functions of ascorbate and glutathione in response of A. verus to Se

Fractionation of hydrolysate from corn germ protein by ultrafiltration: In vitro antidiabetic and antioxidant activity

In the present work, defatted corn germ was hydrolyzed by three proteases and further separated by sequential ultrafiltration with different molecular weight cutoff (100, 10, 2 kDa). Corn germ protein hydrolysate (CGPH) and their fractions were investigated for antioxidant activity, α-glucosidase, α-amylase, and DPP-IV inhibitory activity. The degree of hydrolysis (DH) after 2 hr was 17.5%, 11.14%, and 2.05% for alcalase, trypsin, and flavourzyme, respectively. Trypsin hydrolysate showed the highest DPPH and ABTS+ radical scavenging and Fe2+ chelating activity, but a lower α-glucosidase inhibitory activity. F1 fraction (<2 kDa) exhibited highest radical scavenging and α-glucosidase inhibitory activity. While F2 fraction (2–10 kDa) showed the higher Fe2+ chelating and α-amylase inhibitory activity, F1 fraction of flavourzyme showed the highest α-glucosidase inhibitory and F2 fraction of alcalase and flavourzyme exhibited highest α-amylase inhibitory activity. Hydrolysate and F1 fraction of alcalase and F2 fraction of trypsin showed the highest DPP-IV inhibitory activity. RP-HPLC results showed that trypsin hydrolysate had higher levels of high-hydrophobic peptides. The amino acid composition of the F1 fractions showed high levels of hydrophobic amino acids. Thus, CGPHs may be used as a potential source of antioxidant and antidiabetic peptides in food industry and pharmaceutical application

Fractionation of hydrolysate from corn germ protein by ultrafiltration: In vitro antidiabetic and antioxidant activity

In the present work, defatted corn germ was hydrolyzed by three proteases and further separated by sequential ultrafiltration with different molecular weight cutoff (100, 10, 2 kDa). Corn germ protein hydrolysate (CGPH) and their fractions were investigated for antioxidant activity, α-glucosidase, α-amylase, and DPP-IV inhibitory activity. The degree of hydrolysis (DH) after 2 hr was 17.5%, 11.14%, and 2.05% for alcalase, trypsin, and flavourzyme, respectively. Trypsin hydrolysate showed the highest DPPH and ABTS+ radical scavenging and Fe2+ chelating activity, but a lower α-glucosidase inhibitory activity. F1 fraction (<2 kDa) exhibited highest radical scavenging and α-glucosidase inhibitory activity. While F2 fraction (2–10 kDa) showed the higher Fe2+ chelating and α-amylase inhibitory activity, F1 fraction of flavourzyme showed the highest α-glucosidase inhibitory and F2 fraction of alcalase and flavourzyme exhibited highest α-amylase inhibitory activity. Hydrolysate and F1 fraction of alcalase and F2 fraction of trypsin showed the highest DPP-IV inhibitory activity. RP-HPLC results showed that trypsin hydrolysate had higher levels of high-hydrophobic peptides. The amino acid composition of the F1 fractions showed high levels of hydrophobic amino acids. Thus, CGPHs may be used as a potential source of antioxidant and antidiabetic peptides in food industry and pharmaceutical application