Abstract
Muscle protein functionality plays an important role in routine applications in the food industry. Glycation by the Maillard reaction is a naturally occurring process, which can be used to develop new ingredients with improved functionality using a food grade approach. Actomyosin was conjugated with glucose or glucosamine in a liquid system at moderate temperatures (40°C). Sugar to protein conjugation was evident by UV–Vis spectral changes, with the glycation level determined by matrix assisted laser desorption/ionisation mass spectrometry. Parameters for glycation of muscle protein were optimised using the bidimensional hierarchical clustering analyses. The best glycation conditions were 40°C for 8h at 1:3 protein:sugar ratio. Solubility and emulsifying properties of glycoconjugates were significantly improved as compared to non-glycated proteins. At pH 7 glycated actomyosin was on average 31% more soluble compared to non-treated protein. Glucosamine was found to be more effective for glycation and provided higher protein functionality as compared to glucose.
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