Abstract
The Maillard reaction products (MRPs) between polydextrose (PDX), a popular polysaccharide in formula powder, and β-lactoglobulin (β-LG), a major whey protein, were studied in aggregation degree, structure, hydrophobic, antigenic and antioxidant activity changes of β-LG. Incubation of PDX and β-LG (60 ℃, 79% relative humidity) for up to 72 h yielded MRPs with increases in furosine, UV absorbance, fluorescence intensity and loss of free amino groups. High molecular weight β-LG-PDX MRPs were observed by SDS-PAGE. Circular dichroism spectroscopy revealed negligible change in β-LG secondary structure. Changes in the tertiary structure of β-LG were detected by tryptophan fluorescence spectroscopy consistent with an increase in surface hydrophobicity of heated β-LG-PDX. Antigenicity reduction of β-LG in β-LG-PDX reached its peak when heated for 24 h. After heating for 72 h, DPPH radical-scavenging activity of β-LG-PDX increased by 7.4-fold, and the ferric reducing antioxidant power reached 61.1 µmol ascorbic acid/g protein.
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