(569f) Enzymatic Hydrolysis of Protein to Prepare Active Peptides: From Sequence and Structure to Bioreactor

Enzymatic hydrolysis of protein is an effective way to prepare active peptides. However, the reaction kinetics is so complicated and the hydrolysates distribution is so diverse that it is difficult to quantitatively explain many theoretical problems such as mechanism or dynamics of hydrolysis. In this presentation two model systems, i.e. peptic digestion of bovine hemoglobin (system I) and pancreatic digestion of bovine casein (system II) were systematically investigated by a combination of chromatographic, mass spectrometric and spectroscopic analyses. On the basis of enzyme mechanism and protein structure, the reaction behaviors of protein and release kinetics of peptides have been extensively studied during enzymatic hydrolysis, and a series of researches have been performed from sequence and structure to bioreactor. A set of integrated experimental and theroretical method was formed to analyze the dynamic properties of complex protein enzymatic hydrolysis reaction, which will provide a theoretical basis and have practical value for elucidating the enzyme mechanism, finding the relationship between structure and function of peptides, and optimizing operational conditions or designing novel bioreactor to prepare target active peptides with high yields. These researches are referred to our published papers: (1) Pepsin-induced changes in the size and molecular weight distribution of bovine casein during enzymatic hydrolysis. Journal of Dairy Science, 2007, 90: 5004~5011; (2) Pancreatic hydrolysis of bovine casein: Changes in the size and molecular weight distribution. Food Chemistry, 2008, 107: 151~157; (3) Pancreatic hydrolysis of bovine casein: Identification and release kinetics of phosphopeptides. Food Chemistry, 2007, 104: 276~286; (4) Transformation of antimicrobial into bradykinin-potentiating peptides during peptic hydrolysis of bovine hemoglobin: identification, release kinetics and reaction network of peptides. Journal of the Science of Food and Agriculture, 2007, 87: 461~469; (5) Time-dependent nature in peptic hydrolysis of native bovine hemoglobin. European Food Research and Technology, 2007, 225: 637~647; (6) Identification and release kinetics of peptides from the process of peptic hydrolysis of bovine hemoglobin by LC-ESI-MS/MSU. Preparative Biochemistry & Biotechnology, 2007, 37: 1~16