Corn gluten meal was hydrolyzed with Alcalase 2.4L, an alkaline protease. The effects of enzyme concentration and gluten size reduction on the hydrolysis were studied. Extent of reaction was expressed in terms of both the degree of hydrolysis (using the pH-stat technique) and the concentration of soluble protein. Linear and product inhibition kinetic models were compared to the experimental results after parameter estimation by minimizing the residual sum of squares. The models describe the time-dependent behavior of three protein/peptide pools-insoluble protein, TCA-insoluble proteins, and TCA-soluble peptides. A simplified product inhibition model gave the best fit to the experimental data.