Our previous research indicated that conjugation of whey protein isolates (WPI) with dextran (DX) via the Maillard reaction could provide an alternative approach to decrease the immunogenicity of whey protein. It has been well established that partial enzymatic hydrolysis of proteins also reduces their antigenicity. We want to explore a combination of partial protein hydrolysis and conjugation to decrease whey protein immunogenicity. In this study, we partially hydrolyzed whey protein by immobilized trypsin and chymotrypsin. All the hydrolyzed proteins were then conjugated with dextran (molecular weight 40kDa). Trypsin and chymotrypsin from bovine were immobilized onto (aldehyde) agarose (6% gels). WPI was partially hydrolyzed by these enzymes at 40, 45 and 50°C. Samples of hydrolyzed whey protein at 30, 60, 120, 180 and 240 min of hydrolysis were analyzed by SDS-PAGE and HPLC. The molecular weight of hydrolyzates was measured by Size-exclusion chromatography coupled with multi-angle laser light scattering detector. The degree of hydrolysis (DH) was 5 and 12% after 30 and 180 min respectively of hydrolysis at 50°C. Molecular weights of most hydrolyzates were between 1 to 5 kDa after 180 min hydrolysis at 50°C. Two hydrolyzates with DH values of 5 and 12% were conjugated with 40 kDa molecular weight dextran via our novel aqueous Maillard reaction method. Conjugates were separated and purified by chromatography. The IgE binding capacity was determined by ImmunoCap method using blood serum from cow’s milk protein patient. The IgE binding capacity of conjugated whey protein hydrolyzates is currently being investigated and will be reported. Partial hydrolysis of whey protein plus conjugation with dextran may provide another option to reduce whey protein allergenicity.