Peptides from Alcalase-hydrolyzed soybean protein hydrolysate(SPH)may hold the potential as natural antioxidants.In addition,the effect of human gastrointestinal(GI)tract on peptide bioavailability needs to be explore...Peptides from Alcalase-hydrolyzed soybean protein hydrolysate(SPH)may hold the potential as natural antioxidants.In addition,the effect of human gastrointestinal(GI)tract on peptide bioavailability needs to be explored.In this study,the impact of simulated GI digestion and transepithelial transport on various antioxidant properties of SPH were investigated.SPH displayed DPPH radical scavenging(IC50=4.22 mg/m L),ABTS·+radical scavenging(IC50=2.93 mg/m L),reducing power and metal ion-chelating activities(IC50=0.67 mg/m L).Furthermore,SPH significantly(P<0.05)inhibited the generation of intracellular reactive oxygen species(ROS)in Caco-2 cells.After simulated GI digestion,the antioxidant properties of SPH were enhanced,except for a decrease in ABTS·+radical scavenging activity.After transepithelial transport,the permeates maintained partial antioxidant activity and the LC-MS/MS data further identified the absorbed soybean peptides.These results suggest that SPH contains the antioxidant peptides that are potentially bioavailable and can be regarded as a promising source of functional food ingredients.展开更多
α-lactalbumin (α-LA) might increase its antioxidant potential after hydrolysis. In particular, low molecular weight (LMW) peptides showed greater antioxidant capacity. Different hydrolysis conditions with Alcalase e...α-lactalbumin (α-LA) might increase its antioxidant potential after hydrolysis. In particular, low molecular weight (LMW) peptides showed greater antioxidant capacity. Different hydrolysis conditions with Alcalase enzyme were optimized with a composite central design and surface methodology. Sample obtained after 0.1% (w/w enzyme:substrate), 60 min hydrolysis, ultrafiltrated with membranes of 3 kDa (named 4 LMW), showed the greatest antioxidant values: 1.574 ± 0.060 and 1.636 ± 0.076 μmolTE/mg of protein for ABTS and ORAC-FL, respectively. Sample 4 LMW produced mild ACE inhibition capacity, 22% related to Captopril. 4 LMW was submitted to in vitro gastrointestinal conditions using α-amylase, pepsin, pancreatin and bile-extract;its antioxidant capacity was enhanced by the shorter peptides released, confirmed by SE-HPLC. Antioxidant capacity of digested 4 LMW sample (D 4 LMW) was 1.743 ± 0.086 and 2.542 ± 0.245 μmolTE/mg of protein for ABTS and ORAC-FL, respectively, showing improvement on bioaccessibility. Intestinal cells viability was higher for D 4 LMW.展开更多
基金the financial support received from National Natural Science Foundation of China(No.31430067 and 31601475)China Postdoctoral Science Foundation funded project(No.2017M610200)Postdoctoral Foundation of Heilongjiang Province(No.LBH-Z17011)
文摘Peptides from Alcalase-hydrolyzed soybean protein hydrolysate(SPH)may hold the potential as natural antioxidants.In addition,the effect of human gastrointestinal(GI)tract on peptide bioavailability needs to be explored.In this study,the impact of simulated GI digestion and transepithelial transport on various antioxidant properties of SPH were investigated.SPH displayed DPPH radical scavenging(IC50=4.22 mg/m L),ABTS·+radical scavenging(IC50=2.93 mg/m L),reducing power and metal ion-chelating activities(IC50=0.67 mg/m L).Furthermore,SPH significantly(P<0.05)inhibited the generation of intracellular reactive oxygen species(ROS)in Caco-2 cells.After simulated GI digestion,the antioxidant properties of SPH were enhanced,except for a decrease in ABTS·+radical scavenging activity.After transepithelial transport,the permeates maintained partial antioxidant activity and the LC-MS/MS data further identified the absorbed soybean peptides.These results suggest that SPH contains the antioxidant peptides that are potentially bioavailable and can be regarded as a promising source of functional food ingredients.
文摘α-lactalbumin (α-LA) might increase its antioxidant potential after hydrolysis. In particular, low molecular weight (LMW) peptides showed greater antioxidant capacity. Different hydrolysis conditions with Alcalase enzyme were optimized with a composite central design and surface methodology. Sample obtained after 0.1% (w/w enzyme:substrate), 60 min hydrolysis, ultrafiltrated with membranes of 3 kDa (named 4 LMW), showed the greatest antioxidant values: 1.574 ± 0.060 and 1.636 ± 0.076 μmolTE/mg of protein for ABTS and ORAC-FL, respectively. Sample 4 LMW produced mild ACE inhibition capacity, 22% related to Captopril. 4 LMW was submitted to in vitro gastrointestinal conditions using α-amylase, pepsin, pancreatin and bile-extract;its antioxidant capacity was enhanced by the shorter peptides released, confirmed by SE-HPLC. Antioxidant capacity of digested 4 LMW sample (D 4 LMW) was 1.743 ± 0.086 and 2.542 ± 0.245 μmolTE/mg of protein for ABTS and ORAC-FL, respectively, showing improvement on bioaccessibility. Intestinal cells viability was higher for D 4 LMW.
