Dynamics of evening primrose protein hydrolysis

Evening primrose protein isolate prepared by proteolysis was digested with trypsin at pH 8 and 50 degrees C. Effects of enzyme and substrate concentrations and of digestion time on the degree of protein hydrolysis were determined. Experimental results were used to develop a mathematical model describing the path of enzymatic cleavage of evening primrose protein. According to this model, the process starts with the peptide bond hydrolysis followed either by formation of a stable enzymesubstrate complex or the peptide bond resynthesis, at the constant initial enzyme to substrate 3 concentration ratio (rho(E)o/rho(S)o) and evening primrose protein concentrations of 20 to 50 g dm(-3) Optimum proteolysis conditions (rho(S)o 20 g dm(-3), rho(E)o/rho(S)o = 2 %, 5 h) provided the highest degree of protein hydrolysis of 28-30 Enzymatic digestion enhanced the content of low relative molar mass of peptides (easily absorbable in small intestine) in evening primrose protein hydrolyzate and increased its solubility in water.