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Interface-related attributes of the Maillard reaction-born glycoproteins

ABSTRACT Interfacial behavior of proteins which is a chief parameter to their emulsifying and foaming properties can be tailored through the Maillard reaction. The reaction can increase protein solubility at isoelectric point and ought to be controlled for example by high pressure processing to suppress melanoidins formation. Branched and long saccharides bring considerable steric hindrance which is associated with their site of conjugation to proteins. Conjugation with high molecular weight polysaccharides (such as 440 kDa dextran) may indeed increase the thickness of globular proteins interfacial film up to approximately 25 nm. However, an overly long saccharide can shield protein charge and slow down the electrophoretic mobility of conjugate. Maillard conjugation may decrease the diffusion rate of proteins to interface, allowing further unfolding at interface. As well, it can increase desorption iteration of proteins from interface. In addition to tempering proteins adsorption to interface, Maillard conjugation influences the rheology of protein membranes. Oligosaccharides (especially at higher glycation degrees) decrease the elastic modulus and Huggins constant of protein film; whereas, monosaccharides yield a more elastic interface. Accordingly, glycation of random coil proteins has been exploited to stiffen the corresponding interfacial membrane. Partial hydrolysis of proteins accompanied with anti-solvent-triggered nanoparticulation either before or after conjugation is a feasible way to enhance their emulsifying activity.