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- W2145536290 abstract "► Muscle protein glycation in a liquid medium and at mild temperature was developed. ► Glycation with glucosamine is more efficient as compared to glucose. ► Oxidative changes of muscle protein influence glycation. ► Glycation significantly improves protein functionalities. ► Ammonia liberation is involved in pI shift of glucosamine–glycated actomyosin. 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 8 h 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." @default.
- W2145536290 created "2016-06-24" @default.
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- W2145536290 date "2013-08-01" @default.
- W2145536290 modified "2023-09-26" @default.
- W2145536290 title "Non-enzymatic glycation of natural actomyosin (NAM) with glucosamine in a liquid system at moderate temperatures" @default.
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- W2145536290 doi "https://doi.org/10.1016/j.foodchem.2013.02.026" @default.
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