The generation and application of antioxidant peptides derived from meat protein: a review

Meat and its products, rich in protein, are one of the important potential sources of antioxidant peptides. However, reviews on the generation and application of meat-derived antioxidant peptides are still limited. To understand the research and application progress of meat-derived antioxidant peptides, the main formation pathways and their commercial applications are exhibited, the research methods for the isolation, purification, and identification are summarized, and the influencing factors, evaluation methods, and intestinal absorption pathways are presented in this work. It is summarized that limited degradation by exogenous and endogenous enzymatic hydrolysis is the main pathway for the production of animal-derived antioxidant peptides. Traditional separation, purification, and identification techniques are also applicable to animal-derived antioxidant peptides. The formation of animal-derived antioxidant peptides is affected by many factors, and the intestinal absorption pathways of antioxidant peptides are different. Finally, insufficient and future development directions are provided

ACE Inhibitory Peptides Derived from Muscovy Duck (<i>Cairina moschata</i>) Plasma

In this study, angiotensin-converting enzyme inhibitory peptides (ACE–IPs) derived from Muscovy duck (Cairina moschata) plasma hydrolysate (MDPH) were investigated. According to the general research protocol for bioactive peptides, the crude ACE–IPs of Muscovy duck plasma were separated and purified by ultrafiltration, gel chromatography and reversed-phase high-performance liquid chromatography (RP–HPLC). Then the components with the highest ACE inhibition potential were selected for identification. Finally, the inhibition mechanism was explored by molecular docking and in silico simulated digestion. A total of 121 peptides was detected, and five were screened for synthesis verification and molecular docking. The peptide VALSSLRP revealed high ACE inhibitory activity (91.67 ± 0.73%) because this peptide bound tightly to the S1′ pocket and formed 3 hydrogen bonds. Meaningfully, this work provides some new information about the generation of ACE–IPs derived from duck blood plasma

Content of free and protein-binding Nε-carboxymethyllysine and Nε-carboxyethyllysine in different parts of braised chicken

In order to illustrate the levels of advanced glycation end products (AGEs) in Chinese traditional braised chicken, the distribution of free and protein-binding Nε-carboxymethyllysine (CML) and Nε-carboxyethyllysine (CEL) in four parts of processed chicken including chest (X), leg (T), skin (P), and the mixed whole body (M) was investigated. Our results showed that the content of free CML was 1,186.63–1,795.43 ng/g meat and protein-binding CML was 11,693.91–16,122.90 ng/g meat. Differently, the content of free CEL was 24.81–41.62 ng/g meat and protein-binding CEL was 270.11–385.49 ng/g meat. It was found that the total contents of CML were 31.5–56.8 folds higher than those of CEL. Protein-binding AGEs (CML + CEL) were 6.6–9.9 times higher than those of free AGEs (CML + CEL). Pearson's correlation of AGEs and oxidation in four parts of braised chicken were also investigated, and the results showed that oxidation had a significant effect on levels of CEL; especially, the protein carbonyl was negatively correlated with free CEL (p &lt; .05). TBARs value was significantly positively correlated with protein-binding and total CEL (p &lt; .01). In conclusion, our findings are important for better understanding of the AGEs formation in braised meat

Image_1_Perilla frutescens seed meal as a fat substitute mitigates heterocyclic amine formation and protein oxidation and improves fatty acid profile of pan-fried chicken patties.JPEG

Fatty acid profile, protein and fatty acid oxidation and flavor profile of pan-fried chicken patties formulated with various levels of Perilla frutescens seed meal (PSM) as a fat substitute was investigated in this study. The formation of heterocyclic amines (HCAs) in the chicken patties was also evaluated. The results showed that pan-fried patties formulated with 20% PSM (PSM4) had the highest ranges of oleic acid and ΣMUFA content and ΣPUFA/ΣSFA ratio. Low to medium levels of PSM (PSM1, 2, and 3 corresponding to 5, 10, and 15% of PSM, respectively) reduced the content of lipid peroxidation products, while high level (PSM4) increased it. All levels of PSM were also found to be effective against elevation in carbonyl content relative to the control. Moreover, the PSM effectively inhibited HCA formation in the chicken patties. The total contents of HCAs in PSM1, PSM2, PSM3, and PSM4 samples were significantly (P < 0.05) lower than that of the control sample, corresponding to 31.9, 46.1, 57.2, and 44.8% inhibition, respectively. PSM4, however, had no or very little effect on the formation of PhIP, 4,8-DiMeIQx and AαC, despite a strong inhibitory effect on MeIQx formation. These findings not only support the promising potential of PSM for application as a fat substitute to improve the fatty acid profile and reduce the content of harmful by-products in heat-processed chicken, but also highlight that appropriate addition level is a critical factor in optimizing the functional capacity of this natural agent.</p