Insight into the Mechanism Underlying the Reduction of Digestibility and IgG/IgE Binding Ability in Ovalbumin during Different High-Temperature Conduction Modes-Induced Glycation.

Effects of different high-temperature conduction modes [high-temperature air conduction (HAC), high-temperature contact conduction (HCC), high-temperature steam conduction (HSC)]-induced glycation on the digestibility and IgG/IgE-binding ability of ovalbumin (OVA) were studied and the mechanisms were investigated. The conformation in OVA-HSC showed minimal structural changes based on circular dichroism, fluorescence, and ultraviolet spectroscopy. The degree of hydrolysis analysis indicated that glycated OVA was more resistant to digestive enzymes. Liquid chromatography-Orbitrap mass spectrometry identified 11, 14, and 15 glycation sites in OVA-HAC, OVA-HCC, and OVA-HSC, respectively. The IgG/IgE-binding ability of OVA was reduced during glycation and digestion, and the interactions among glycation, allergenicity, and digestibility were further investigated. Glycation sites masked the IgG/IgE epitopes resulting in a reduction in allergenicity. Digestion enzymes destroyed the IgG/IgE epitopes thus reducing allergenicity. Meanwhile, the glycation site in proximity to the digestion site of pepsin was observed to cause a reduction in digestibility.

Comparison of ovalbumin glycation induced by high-temperature steaming and high-temperature baking: A study combining conventional spectroscopy with high-resolution mass spectrometry.

High-temperature steaming (HTS) and high-temperature baking (HTB)-induced ovalbumin (OVA)-glucose glycation (140 °C, 1-3 min) were compared, and the different mechanisms were evaluated by changes in protein conformation, glycation sites and average degree of substitution per peptide molecule (DSP) values as well as the antioxidant activity of glycated OVA. Conventional spectroscopic results suggested that in comparison with HTB, HTS promoted protein expansion, increased ß-sheet content and made OVA structure more orderly. Liquid chromatography-high resolution mass spectrometry (LC-HRMS) analysis showed that 10 glycation sites were found under HTB, while 4 new glycation sites R111, R200, R219 and K323 appeared under HTS, and 2 of them (R219 and K323) were located in internal ß-sheet chains. The antioxidant activities of glycated OVA increased with increasing treatment time, and HTS showed stronger enhancement effect than HTB. Furthermore, the DSP values were generally higher under HTS than HTB. Compared with HTB, HTS with high penetrability could enhance the change of OVA primary structure and spatial conformation, making the protein structure more unfolded and stable, leading to more protein-sugar collisions occurred in inner OVA molecular and significantly promoted glycation. In conclusion, HTS is a promising method for high-temperature short-time glycation reaction, with drastically increasing the protein antioxidant activities.

Effects of different high-temperature conduction modes on the ovalbumin-glucose model: AGEs production and regulation of glycated ovalbumin on gut microbiota.

Food high-temperature processing frequently induces the production of advanced glycation end products (AGEs) in the food industry. In this study, the effects of three high-temperature conduction modes on the AGEs production derived from ovalbumin (OVA)-glucose model and the regulation of glycated OVA on gut microbiota were investigated. The peak time of OVA shifted maximally from 13.72 to 13.57 due to the rise in molecular weight, confirming successful coupling between OVA and glucose. The inhibition of superheated steam (SS) on AGEs was observed, with the sample treated by SS showing the lowest content among glycated OVA groups. The analysis revealed an increase in AGEs during digestion and a decrease in fermentation, suggesting the release during digestion and the availability by intestinal flora. Furthermore, an expansion of Bifidobacterium and Lactobacillus, and the inhibition of Desulfovibrio and Escherichia-Shigella were observed, indicating the prebiotic activity of glycated OVA and its potential to improve intestinal health. These results provide valuable information for controlling high-temperature processing to inhibit AGEs formation and highlight the positive effects of glycated proteins on intestinal health.

eIF3 mRNA selectivity profiling reveals eIF3k as a cancer-relevant regulator of ribosome content.

eIF3, whose subunits are frequently overexpressed in cancer, regulates mRNA translation from initiation to termination, but mRNA-selective functions of individual subunits remain poorly defined. Using multiomic profiling upon acute depletion of eIF3 subunits, we observed that while eIF3a, b, e, and f markedly differed in their impact on eIF3 holo-complex formation and translation, they were each required for cancer cell proliferation and tumor growth. Remarkably, eIF3k showed the opposite pattern with depletion promoting global translation, cell proliferation, tumor growth, and stress resistance through repressing the synthesis of ribosomal proteins, especially RPS15A. Whereas ectopic expression of RPS15A mimicked the anabolic effects of eIF3k depletion, disruption of eIF3 binding to the 5'-UTR of RSP15A mRNA negated them. eIF3k and eIF3l are selectively downregulated in response to endoplasmic reticulum and oxidative stress. Supported by mathematical modeling, our data uncover eIF3k-l as a mRNA-specific module which, through controlling RPS15A translation, serves as a rheostat of ribosome content, possibly to secure spare translational capacity that can be mobilized during stress.