Journal of the Science of Food and Agriculture · 2015 · 91 citations · 43 references
AgricultureBiochemistryFood ScienceCereal ScienceFood ChemistryFood ProcessingGlycan AnalysisProtein AnalysisProtein GlycoengineeringProteins In FoodsCoiled-coil StructureEmulsificationEmulsification MechanismsHydrophobicityPhysicochemical PropertiesProtein-sugar InteractionsSurface Hydrophobicity EffectsUltrasound Processing Effects
BACKGROUND: The objective of this study was to determine the effect of ultrasound treatment on the wet heating Maillard reaction between mung bean protein isolates (MBPIs) and glucose, and on structural and physico-chemical properties of the conjugates. RESULTS: The degree of glycosylation of MBPI-glucose conjugates treated by ultrasound treatment and wet heating (MBPI-GUH) was higher than that of MBPI-glucose conjugates only treated by wet heating (MBPI-GH). Solubility, emulsification activity, emulsification stability and surface hydrophobicity of MBPI-GUH were higher than that of MBPI-GH. Grafted MBPIs had a lower content of α-helix and unordered coil, but a higher content of β-sheet and β-turn structure than MBPIs. No significant structural changes were observed in β-turn and random coil structure of MBPI-GUH, while α-helix content increased with ultrasonic time, and decreased at 300 W ultrasonic power with the increase of β-sheet. MBPI-GUH had a less compact tertiary structure compared to MBPI-GH and MBPI. Grafting MBPIs with glucose formed conjugates of higher molecular weight, while no significant changes were observed in electrophoresis profiles of MBPI-GUH. CONCLUSION: Ultrasound-assisted wet heating Maillard reaction between MBPIs and glucose could be a promising way to improve functional properties of MBPIs.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations