The aim of this study was to select potential probiotic yeasts from dry-cured Xuanwei ham and investigate yeast-derived antioxidant peptides. The results showed that two strains (XHY69 and XHY79) were selected as potential probiotic yeasts and identified as Yamadazyma triangularis. The two yeasts showed tolerance under pH 2.5 and 1% bile salt, in addition to protease activity, auto-aggregation, antibacterial, and antioxidant activities. The peptide fraction (MW < 3 kDa) isolated from XHY69 fermentation broth, named XHY69AP, showed higher radical scavenging activities than glutathione at a concentration of 4.5 mg/mL (p < 0.05). The fraction (AP-D10) was purified from XHY69AP by gel filtration chromatography and reversed-phase high performance liquid chromatography, and then further identified by a UHPLC-LTQ-Orbitrap mass spectrometer. The molecular weight of all 55 purified sequences was distributed between 0.370 and 0.735 kDa. Among these seven novel peptides, Tyr-Pro-Leu-Pro (YPLP), Ala-Gly-Pro-Leu (AGPL), Gly-Pro-Phe-Pro (GPFP), and Ala-Pro-Gly-Gly-Phe (APGGF) were identified. All sequences were abundant in hydrophobic amino acids, especially proline residue. Among these novel peptides, YPLP possessed the highest ABTS scavenging rate (75.48%). The present work selects two new probiotic potential yeasts from dry-cured Xuanwei ham that are effective to yield novel antioxidant peptides.

Lipid oxidation and protein oxidation occur side by side in meat. Here, the effect of malondialdehyde (MDA), the major product of lipid oxidation, on the digestibility of beef myofibrillar proteins (MP) was studied. MP samples were incubated with 0, 0.1, 0.3, 0.5, and 0.7 mM MDA at 4 °C for 12 h and then subjected to in vitro gastrointestinal digestion. The result showed that MDA remarkably reduced the digestibility of MP (p < 0.05). MDA treatments significantly increased carbonyl and Schiff base contents in MP (p < 0.05). The microstructure observed by atomic force microscopy showed that MDA treatments resulted in the aggregation of MP. Non-reducing and reducing electrophoresis suggested the aggregation was mainly caused by covalent bonds including disulfide bond and carbonyl–amine bond. Proteomics analysis proved that the myosin tail was the main target of MDA attack, meanwhile, lysine residues were the major modification sites. Taken together, the above results imply that MDA induces protein oxidation, aggregation, and blockage of hydrolysis sites, consequently leading to the decrease in both gastric and gastrointestinal digestibility of MP.

This study aimed to investigate the effect of oxidized beef protein on colon health. C57BL/6 mice were fed diets containing in vitro oxidized beef protein (carbonyl content 5.83/9.02 nmol/mg protein) or normal beef protein (control group, carbonyl content 2.27 nmol/mg protein) for 10 weeks. Histological observations showed that oxidized beef protein diet induced notable inflammatory cell infiltrations in colon. The analysis of high-throughput sequencing indicated oxidized beef protein largely altered the composition of gut microbiota (GM) by increasing proinflammatory bacteria (Desulfovibrio, Bacteroides, Enterorhabdus) while reducing beneficial bacteria (Lactobacillus, Akkermansia). In addition, oxidized beef protein remarkably increased protein fermentation in the colon, which was evidenced by the elevated i-butyrate, i-valerate, and ammonia levels in feces. Furthermore, consuming oxidized beef protein destroyed colon barrier functions by decreasing tight junction proteins expression. These changes in colonic ecosystem activated the proinflammatory pathway of lipopolysaccharide/toll-like receptor-4/nuclear factor kappa B (LPS/TLR-4/NF-κB), eventually leading to colonic inflammatory damage in mice. Taken together, these results imply that consuming oxidized beef protein detrimentally regulates GM and impairs colon health.

No abstract

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 <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.