β-Lactoglobulin conformation and mixed sugar beet pectin gel matrix is changed by laccase

- Laccase treated BLG changed RMS distribution profile from sphere to random coil.
- No increase in MW observed in laccase treated BLG.
- BLG polymerization was more enhanced by heat treatment in the presence of laccase.
- Increased MW and decreased ferulic acid was observed in BLG and SBP complexes.
- BLG might be entrapped in SBP matrix.

Sugar beet pectin (SBP) and β-lactoglobulin (BLG) contain ferulic acid and tyrosine, respectively, potential substrates for laccase. Dispersions of BLG were treated with laccase and/or heat and SBP to assess potential for ferulic acid in SBP to influence laccase conjugation of BLG. Changes were investigated by size exclusion chromatography combined with multi angle laser light scattering (HPSEC-MALLS), refractive index (RI) and UV detector, particle size and ζ-potential analysis. Molecular weight (MW) of BLG decreased from 3.7 × 104 to 2.9 × 104 and root mean square (RMS) decreased from 41 to 36 after laccase treatment. The slope of a conformation plot increased from 0.35 to 0.72, indicating a change in shape in laccase treated BLG to more random coil. While laccase did not affect MW of BLG, MW of BLG increased after sequential heat and laccase treatment to 2.9 × 106 and 4.4 × 106, respectively. Free thiol (SH) increased by heat and laccase treatment of BLG; tyrosine in BLG increased only by heat. An increased MW and decreased ferulic acid in SBP was observed in the presence of BLG and laccase. The increase in MW was attributed to entrapment of BLG in SBP cross-linked matrix catalyzed by laccase.