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Rapid Formation of Biologically Active Neoglycoprotein from Lysozyme and Xyloglucan Hydrolysates through Naturally Occurring Maillard Reaction
14
Citations
2
References
2000
Year
EngineeringGlycobiologyProtein MoleculePolysaccharideEnzymatic ModificationFood ChemistryOccurring Maillard ReactionBiochemical EngineeringHen Egg-white LysozymeGlycosylationProtein GlycosylationBiochemistryBiomolecular EngineeringRapid FormationNatural SciencesBiotechnologyBiologically Active NeoglycoproteinGlycol ChitinProtein EngineeringHemicelluloseCarbohydrate-protein Interaction
Hen egg-white lysozyme was conjugated with 7~9 mers xyloglucan hydrolysates (MW=1,400) at 60℃ and 79% relative humidity for 3 days. SDS-PAGE showed that the conjugation between lysozyme and the oligosaccharide began from 1-day incubation, and three molecules of carbohydrate chains were attached to a protein molecule after 3-day incubation. The enzymatic activity of lysozyme was totally conserved in the neoglycoprotein, when measured by using glycol chitin as substrate. Besides, the emulsifying properties of lysozyme were vastly improved by the conjugation with the oligosaccharide, in which emulsifying activity of the neoglycoprotein was five times higher than that of native one.
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