Abstract: Differential scanning calorimetry and circular dichroism were used to analyze the conformational change of trypsin induced by dynamic high-pressure microfluidization (DHPM) .Based on the reflection in conformational change of the unfolding trypsin induced by DHPM in our previous study, the conformation of native and unfolding trypsin was predicted and modeled by PyMOL and 3DS Max.The results indicated that compared with native trypsin, the decrease in thermal enthalpy and the change of percentages of secondary structural elements, the loose structure of unfolding trypsin was found.The active center, disulfide bond and the secondary structural information of trypsin was visually viewed by the modeled conformation figure.In addition, preliminary study on the structural modeling change of DHPM-induced unfolding trypsin was completed.