It was shown that limited enzymatic hydrolysis of wheat storage protein yielded hydrolysates with valuable functional properties for food uses. To develop an industrially efficient process to perform this hydrolysis, studies have been carried out in a torus reactor. In the investigation, limited hydrolysis of native gliadin by pepsin was carried out in a 2.11 torus reactor, to study the effect of operating conditions on tile degree of hydrolysis. The results are discussed and compared with those obtained in a batch-stirred reactor (part 1 of this series), The comparison of the performance of both types of reactor is made by using a criterion based on the power per unit volume and the concentration of peptide bonds cleaved during the hydrolysis process. Finally, a model of plug flow with recirculation is proposed to characterize the performance of the limited enzymatic hydrolysis of native gliadin in the torus reactor.