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The demand for plant-based meat analogs (PBMA) is on the rise as a strategy to sustain the food protein supply while mitigating environmental change. In addition to supplying essential amino acids and energy, food proteins are known sources of bioactive peptides. Whether protein in PBMA affords similar peptide profiles and bioactivities as real meat remains largely unknown. The purpose of this study was to investigate the gastrointestinal digestion fate of beef and PBMA proteins with a special focus on their potential as precursors of bioactive peptides. Results showed that PBMA protein showed inferior digestibility than that in beef. However, PBMA hydrolysates possessed a comparable amino acid profile to that of beef. A total of 37, 2420 and 2021 peptides were identified in the gastrointestinal digests of beef, Beyond Meat and Impossible Meat, respectively. The astonishingly fewer peptides identified from beef digest is probably due to the near-full digestion of beef proteins. Almost all peptides in Impossible Meat digest were from soy, whereas 81%, 14% and 5% of peptides in Beyond Meat digest were derived from pea, rice and mung proteins, respectively. Peptides in PBMA digests were predicted to exert a wide range of regulatory roles and were shown to have ACE inhibitory, antioxidant and anti-inflammatory activities, supporting the potential of PBMA as a source of bioactive peptides.

This present study aimed to investigate the effects of various cooking times (1 h, 1.5 h, 2 h, 2.5 h, named as JHBP-1, JHBP-1.5, JHBP-2, JHBP-2.5) on the antioxidant activity and peptide profile of Jinhua ham broth peptides (JHBP). The peptides extracted from uncooked ham were used as an uncooked group with the name of JHBP-0. The results revealed that the antioxidant efficacy in the four cooked groups changed dramatically compared to JHBP-0. After cooking, the DPPH radical scavenging activity, hydroxyl radical scavenging activity and superoxide anion radical scavenging activity decreased, except for the Fe2+ chelation and ABTS+ scavenging capacity which increased significantly. However, the cooked groups still showed a strong antioxidant capacity. In particular, the superoxide anion radical scavenging ability and the Fe2+ chelation action were significantly stronger compared to glutathione (GSH) and butylated hydroxytoluene (BHT) (p < 0.05). JHBP-1.5 also displayed stronger antioxidant capacity than the other three cooked groups, and its secondary structure and mass distribution changed significantly after cooking, specifically with an increased proportion of helix and

The study aimed to analyze pH and heat treatment’s effect in modulating the release of peptides with antioxidant activity after simulated gastrointestinal (GI) digestion of Egg white powder (EWP). EWP samples with neutral (EWPN) and alkaline (EWPA) pH were heat-treated at 20, 60, and 90 °C and analyzed for protein aggregation, solubility, and GI digestibility. Heat treatment decreased solubility and induced protein aggregation, which was higher for EWPN as compared to EWPA. The unfolding of EWPA proteins at 60 °C exhibited a higher GI digestibility and antioxidant activity via Oxygen Radical Absorbance Capacity (ORAC) assay as compared to EWPN. Interestingly, a reverse trend was observed in the cellular antioxidant assay, and the GI-digest of EWPN exhibited a higher antioxidant activity. The LC-MS/MS analysis are in concordance with cellular antioxidant activity assay and showed a higher intensity for peptides with potential antioxidant activity in the GI-digest of EWPN. The results indicate that heat treatment but not the pH is a critical factor in improving the protein digestibility and releasing peptides with antioxidant activity after GI digestion.

The demand for plant-based meat analogs (PBMA) is on the rise as a strategy to sustain the food protein supply while mitigating environmental change. In addition to supplying essential amino acids and energy, food proteins are known sources of bioactive peptides. Whether protein in PBMA affords similar peptide profiles and bioactivities as real meat remains largely unknown. The purpose of this study was to investigate the gastrointestinal digestion fate of beef and PBMA proteins with a special focus on their potential as precursors of bioactive peptides. Results showed that PBMA protein showed inferior digestibility than that in beef. However, PBMA hydrolysates possessed a comparable amino acid profile to that of beef. A total of 37, 2420 and 2021 peptides were identified in the gastrointestinal digests of beef, Beyond Meat and Impossible Meat, respectively. The astonishingly fewer peptides identified from beef digest is probably due to the near-full digestion of beef proteins. Almost all peptides in Impossible Meat digest were from soy, whereas 81%, 14% and 5% of peptides in Beyond Meat digest were derived from pea, rice and mung proteins, respectively. Peptides in PBMA digests were predicted to exert a wide range of regulatory roles and were shown to have ACE inhibitory, antioxidant and anti-inflammatory activities, supporting the potential of PBMA as a source of bioactive peptides.

This present study aimed to investigate the effects of various cooking times (1 h, 1.5 h, 2 h, 2.5 h, named as JHBP-1, JHBP-1.5, JHBP-2, JHBP-2.5) on the antioxidant activity and peptide profile of Jinhua ham broth peptides (JHBP). The peptides extracted from uncooked ham were used as an uncooked group with the name of JHBP-0. The results revealed that the antioxidant efficacy in the four cooked groups changed dramatically compared to JHBP-0. After cooking, the DPPH radical scavenging activity, hydroxyl radical scavenging activity and superoxide anion radical scavenging activity decreased, except for the Fe 2+ chelation and ABTS + scavenging capacity which increased significantly. However, the cooked groups still showed a strong antioxidant capacity. In particular, the superoxide anion radical scavenging ability and the Fe 2+ chelation action were significantly stronger compared to glutathione (GSH) and butylated hydroxytoluene (BHT) ( p < 0.05). JHBP-1.5 also displayed stronger antioxidant capacity than the other three cooked groups, and its secondary structure and mass distribution changed significantly after cooking, specifically with an increased proportion of helix and <1 kDa peptides. Moreover, the constitution of free amino acids (FAAs) and the types of peptides released in the broth increased significantly with a longer cooking time. In total, 1306 (JHBP-0), 1352 (JHBP-1), 1431 (JHBP-1.5), 1500 (JHBP-2), and 1556 (JHBP-2.5) peptide sequences were detected using LC-MC/MC. The proportion of <1 kDa peptides also gradually increased as the cooking time extended, which is consistent with the molecular weight distribution measurements.

The study aimed to analyze pH and heat treatment's effect in modulating the release of peptides with antioxidant activity after simulated gastrointestinal (GI) digestion of Egg white powder (EWP). EWP samples with neutral (EWPN) and alkaline (EWPA) pH were heat-treated at 20, 60, and 90 °C and analyzed for protein aggregation, solubility, and GI digestibility. Heat treatment decreased solubility and induced protein aggregation, which was higher for EWPN as compared to EWPA. The unfolding of EWPA proteins at 60 °C exhibited a higher GI digestibility and antioxidant activity via Oxygen Radical Absorbance Capacity (ORAC) assay as compared to EWPN. Interestingly, a reverse trend was observed in the cellular antioxidant assay, and the GI-digest of EWPN exhibited a higher antioxidant activity. The LC-MS/MS analysis are in concordance with cellular antioxidant activity assay and showed a higher intensity for peptides with potential antioxidant activity in the GI-digest of EWPN. The results indicate that heat treatment but not the pH is a critical factor in improving the protein digestibility and releasing peptides with antioxidant activity after GI digestion.