FUNCTIONAL IMPROVEMENT OF BETA-LACTOGLOBULIN BY CONJUGATING WITH ALGINATE LYASE-LYSATE

Bovine beta-lactoglobulin-alginic acid oligosaccharide (beta-LG-ALGO) conjugate was prepared by the Maillard reaction to improve the functio n of beta-LG. The molar ratio of beta-LG to ALGO in the conjugates was 1:7. The isoelectric point of the conjugate was 4.55, which is lower than that of beta-LG. Fluorescence studies suggested that the conforma tion around Trp had changed in the conjugate and that the surface of t he conjugate was covered with saccharide chain. Structural analyses wi th monoclonal antibodies indicated that the conformation around Va115- Ile29 (beta-sheet) in the conjugate had changed, while native structur e was maintained around Thr125-Lys135 (alpha-helix). By conjugation wi th ALGO, beta-LG was endowed with high heat stability. The emulsifying activity and the aggregating property of beta-LG was improved in the conjugate.