ArticleFood science & nutrition2021
Effect of methylglyoxal on the alteration in structure and digestibility of α-lactalbumin, and the formation of advanced glycation end products under simulated thermal processing.
Article in Food science & nutrition, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Lipid oxidation-mediated non-enzymatic glycation and its impact on the digestibility of milk proteins.Frontiers in nutrition · 2026Article
- Modifications of the Structural, Nutritional, and Allergenic Properties of Atlantic Cod Induced by Novel Thermal Glycation Treatments.Foods (Basel, Switzerland) · 2024Article
- Insights into the Mechanism Underlying the Influence of Glycation with Different Saccharides and Temperatures on the IgG/IgE Binding Ability, Immunodetection, In Vitro Digestibility of Shrimp (Foods (Basel, Switzerland) · 2023Article
- Protein carbonylation in food and nutrition: a concise update.Amino acids · 2022Article
- Effect of methylglyoxal on the alteration in structure and digestibility of α-lactalbumin, and the formation of advanced glycation end products under simulated thermal processing.Food science & nutrition · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Dicarbonyl compounds (α-DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α-DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α-DCs, was selected to investigate the alteration effects on the structure and digestibility of α-lactalbumin (αLA) under thermal processing (60-100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High-resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and N
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Registered trials
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