Enzymatic hydrolysis of wheat proteins Part I. Enzymatic kinetics and study of limited hydrolysis in a batch stirred reactor

Gliadin peptides obtained by limited enzymatic hydrolysis were produced for their original properties. Experimental determination of the kinetic constants, Km and Vmaxwas carried out to characterize the affinity of pepsin for native gliadin and to allow the performance prediction of the bioreactors in which the reaction is performed. Limited hydrolysis of native gliadin by pepsin in a batch stirred reactor was realized to study the effect of substrate concentration and impeller speed on the concentration of the free amino-acid group (-NH(2),) obtained, and consequently on the degree of hydrolysis (DH) On the other hand, the resulting reaction products were qualitatively analysed by electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) and reversed-phase high performance liquid chromatography (RI’-HPLC)