The relationship between proteolysis and texture in Feta-type cheese made from ultrafiltered cows' milk was studied using capillary electrophoresis, chemical analysis and uniaxial compression. For this purpose cheeses were made with almost identical gross chemical compositions, but wide variations in texture, obtained by varying the amount of rennet and the coagulation conditions. αs1-Casein (CN) 8P, αs1-CN 9P and αs1-CN 8P-I were degraded during ripening, while β-CN A1, β-CN A2 and para-κ-CN were slightly degraded at the highest rennet additions and longest storage time tested (39 weeks). αs1-CN 8P, αs1-CN 9P and αs1-CN 8P-I were degraded even in cheeses made without rennet, and this was ascribed to cathepsin D activity. αs1-CN 9P disappeared faster than αs1-CN 8P, which suggests that milk acid phosphatase was active during storage. During ripening, stress at fracture (σf), strain at fracture (εf), the deformability modulus (E) and work to fracture (Wf) all decreased. Since the gross chemical composition was essentially constant during storage, these changes could be ascribed purely to proteolysis. Although εf could be predicted fairly well from capillary electrophoresis results (correlation coefficient 0·85), there were no unique relationships between degradation of casein components and σf when both storage time and the amount of rennet used were varied. In the young cheese a high level of proteolysis could coexist with high values of σf. This suggests that high levels of rennet caused σf to increase, via an effect unrelated to general proteolysis, whereas general proteolysis caused the reverse effect.