Inhibition of Maillard Reactions by Replacing Galactose with Galacto-Oligosaccharides in Casein Model Systems

Lactose reduced dairy products are more prone to Maillard reactions due to the presence of reactive monosaccharides. Conventional beta-galactosidases, which are used for lactose hydrolysis in lactose-reduced dairy products, will lead to conversion of lactose into glucose and galactose, where especially galactose is very reactive during Maillard reactions. Some beta-galactosidases have transgalactosylating activity and will thus convert lactose into galacto-oligosaccharides (GOS) and hereby limit the release of galactose. The aim of this study was to investigate the extent of participation of GOS in Maillard reactions in comparison to lactose, a 50:50 mixture of glucose and galactose, and galactose exclusively in sodium caseinate-based milk-like model systems heated at 130 and 75 degrees C at pH 6.8. The GOS system exhibited reduced loss of free amino groups; accumulated less furosine and less of the following advanced glycation end products (AGEs): N-epsilon-carboxyethyl lysine, methylglyoxal-derived hydroimidazolone isomers, glyoxal-derived lysine dimer, and methylglyoxal-derived lysine dimer; and also developed less browning compared to monosaccharide models. However, the GOS-caseinate system accumulated more 3-deoxyglucosone and 3-deoxygalactosone, which resulted in higher concentrations of 5-(hydroxymethyl)furfural and pyrraline. The results indicated that GOS overall participate less readily in Maillard reactions than the monosaccharides investigated but were more prone to degradation to C6 alpha-dicarbonyls species. Finally, relationship analysis indicated that C6 alpha-dicarbonyls seemed to primarily increase concentrations of 5-(hydroxymethyl)furfural instead of AGEs. Our results suggest that conversion of lactose into GOS instead of monosaccharides in milk by transgalactosylating beta-galactosidases could be a useful strategy for production of lactose-free milk for people with lactose intolerance.