Microwave-assisted maillard reaction between rice protein and dextran induces structural changes and functional improvements

Glycated α-lactalbumin based micelles for quercetin delivery: Physicochemical stability and fate of simulated digestion

“…Moreover, with larger proportion of dextran, the intensity at amide II gradually disappeared. These changes were similarly described by previous studies, suggesting the consumption of –NH 2 groups and the generation of Schiff base (C N) ( Cheng, Mu, Jiao, Xu, & Chen, 2021 ). The absorptions caused by consecutive α-glucopyranose rings in the structure of dextran were stronger in glycated products than ALA, but weaker than mixtures, which also indicated successful attachment of dextran to ALA ( Liu et al, 2021 ).…”

Insight into the incredible effects of microwave heating: Driving changes in the structure, properties and functions of macromolecular nutrients in novel food

“…Because high quantities of dextran crowd the system and produce steric hindrance, which prevents excessive denaturation. For example, after the Maillard reaction was triggered by microwave, no substantial modifications in the secondary structure of rice protein were identified ( 67 ). Furthermore, the Maillard process was discovered to transform the protein structure from disorder to order to some extent.…”

“…At the same time, under the high-power microwave treatment, the protein expands, which increases the probability of effective collision between it and sugar molecules, enhancing the Maillard reaction ( 95 ). For example, the activation energy of RP-dextran Maillard reaction of rice protein treated by microwave was lower than that of conventional heating ( 67 ). The Maillard reaction products can improve flavor, some can increase the antioxidant capacity and reduce the damage caused by peroxide to the body, but there are also some reaction products that are carcinogenic and harmful to the body's health.…”

Effect of ultrasound on the glycosylation reaction of pea protein isolate–arabinose: Structure and emulsifying properties

“…The protein is sensitive to environmental factors such as temperature and acid, and many studies have focused on the group modification of PPI. Glycosylation (Maillard reaction), a naturally occurring reaction of proteins and reducing sugars under heating conditions, has been explored to improve functional properties, especially solubility and the surface properties of proteins [11] , [12] . Dickinson et al [13] found that during glycosylation, reducing sugars are covalently bound to proteins so that proteins are protected under low pH and high ionic strength solution, improving protein solubility and stability [14] .…”