title: Laccase mediated conjugation of heat treated β-lactoglobulin and sugar beet pectin.
abstract: 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.
authors.affiliation: Department of Food Science and Technology, University of Georgia, Athens, GA, United States.
authors.forename: Jiyoung
authors.initials: J
authors.lastname: Jung
authors.forename: Louise
authors.initials: L
authors.lastname: Wicker
mesh_terms: D027461:Beta vulgaris / Q000737:chemistry*; D006358:Hot Temperature; D042845:Laccase / Q000737:chemistry*; D007782:Lactoglobulins / Q000737:chemistry*; D010368:Pectins / Q000737:chemistry*; D012995:Solubility
chemical_list: D007782:Lactoglobulins; D010368:Pectins; D042845:Laccase