Laccase, an oxidative enzyme, was used to catalyze the hetero and homo covalent conjugation between ferulic acid in sugar beet pectin (SBP) and tyrosine in heated β-lactoglobulin (H_BLG). The conjugation of SBP and H_BLG was confirmed by peak position using size exclusion chromatography, multi angle laser light scattering, refractive index, and UV detection. H_BLG, pre-treated with laccase, eluted at an earlier volume with greater UV280 absorbance than non-laccase treated dispersions. Tyrosine decreased in H_BLG that contained laccase treated SBP samples. Heat enhanced exposure of tyrosine in BLG and improved conjugation with SBP by laccase. H_BLG·SBP conjugates with laccase had improved solubility than laccase untreated dispersions at pH values near the isoelectric point of BLG.
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