A new method was used to analyze

characterize and simulate the kinetic behavior of bio-macromolecular enzymatic hydrolysis reaction based on bio-informatics

HPSEC and graphic processing. Tryptic hydrolysis of whole casein was selected as a model system. The possible reaction mechanism was deduced from a series of chromatographic results and experimental analysis. According to programming calculation and molecular simulation

product information

such as cleavage sites of protein and structure model of active peptides

was also obtained. Furthermore

a 3-D continuous surface and corresponding contour were plotted to characterize the dynamic process of protein enzymatic hydrolysis

and mathematical analysis of the surface-fit function was also carried out. The optimized polynominal equation can be applied to adjustment and control of the complex reaction. It is also beneficial to directional and quantitative preparation of target active peptides.