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Our previous research revealed that dynamic high pressure microfluidization(DHPM)increased the antigenicity of β-lactogloblin(β-Lg)below 80 Mpa,which was related to the unfolding of protein.To test the hypothesie that the unfolding of protein may change proteolytic susceptibility of β-Lg and modulate its antigenicity during the digestion,we developed that the steady-state kinetics of tryptic hydrolysis of β-Lg subjected to DHPM(0.1-80 MPa)have been investigated in relation with the antigenicity in this study.According to the steady-state kinetics analysis,the improved digestion of β-Lg was accompanied with the obvious decrease of antigenicity during the hydrolysis with pressure increasing,reflected by the increase of kc,the decrease of Km,the increase of over-all catalytic efficiency(kc/Km),and the increase of the binding volume.It was indicated that although DHPM can increase the antigenicity of β-Lg,the enhanced digestibility of β-Lg at elevated pressure contributed to a decrease of antigenicity during the hydrolysis.