PHIP

This study investigated the effect of immersion time of chicken breasts in potato starch (PS) coating containing amino acids (AAs) on the formation of 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine (PhIP) and to evaluate a possible mechanism to inhibit the formation of PhIP in chicken breasts during frying. The chicken breasts with standardized dimensions were dipped in the potato starch (PS) coating solution containing 0.25% w/v lysine (Lys) for different times (15 min, 30 min, 1 h, 3 h, and 6 h). After drying the coating on the chickens, samples were fried at 195 °C for 7.5 min on each side. Results showed that the immersion time does not significantly decrease (p < 0.05) the PhIP level, suggesting that 15 min immersion time is enough for PhIP reduction compared to the control chicken samples (without coating). Phenylacetaldehyde (PheAce) was increased in chicken breast coated with PS-0.25% Lys after frying, suggesting that there should be another pathway to prevent the formation of PhIP by the addition of PS-0.25% Lys. Volatile compound analysis also confirmed this and showed increases in many aroma compounds in the coated chicken. Moreover, no significant differences (p < 0.05) were shown between the cooking loss percentage, color parameters, texture profile, and tenderness of chicken with the PS-0.25% coating and chicken without coating.

DDB1- and CUL4-associated factors (DCAFs) CDT2 and DCAF14 are substrate receptors for Cullin4-RING E3 ubiquitin ligase (CRL4) complexes. CDT2 is responsible for PCNA-coupled proteolysis of substrates CDT1, p21, and SET8 during S-phase of cell cycle. DCAF14 functions at stalled replication forks to promote genome stability, but the mechanism is unknown. We find that DCAF14 mediates replication fork protection by regulating CRL4^CDT2 activity. Absence of DCAF14 causes increased proteasomal degradation of CDT2 substrates. When forks are challenged with replication stress, increased CDT2 function causes stalled fork collapse and impairs fork recovery in DCAF14-deficient conditions. We further show that stalled fork protection is dependent on CDT2 substrate SET8 and does not involve p21 and CDT1. Like DCAF14, SET8 blocks nuclease-mediated digestion of nascent DNA at remodeled replication forks. Thus, unregulated CDT2-mediated turnover of SET8 triggers nascent strand degradation when DCAF14 is absent. We propose that DCAF14 controls CDT2 activity at stalled replication forks to facilitate SET8 function in safeguarding genomic integrity.

The heterocyclic amine 2-amino-1-methyl-6-phenyl-imidazolium [4, 5-B] pyridine (PhIP), commonly found in roasted meat products, is considered a potential carcinogen. This study is to explore the underlying mechanisms involved in the adsorption of PhIP by lactic acid bacteria 37X-15 and its peptidoglycan. The scanning electron microscope results suggested that the strain's adsorption on PhIP occurs on the cell wall, primarily composed of peptidoglycan. The fourier-transformed infrared spectroscopy results indicated that PhIP adsorption by both lactic acid bacteria 37X-15 and its peptidoglycan primarily involved OH and NH binding groups. Different adsorption conditions affected the adsorption rate of PhIP by peptidoglycan. The optimal values for each adsorption condition were 2 h, 37 °C, and pH 6 when the maximum adsorption rate reached. This study provides a new direction for the application of lactic acid bacteria and its peptidoglycan in food safety.