Isoelectric focusing and 2-dimensional electrophoresis were used to study the development of the pH 4·6-insoluble fraction during Camembert cheese ripening. Modifications of this fraction were due mainly to the action of 5 proteinases: rennet (chymosin + bovine pepsin), plasmin and Penicillium caseicolum aspartyl-and metalloproteinases. Rennet was inactive on β-casein, but acted very early on αs1-casein. However, rennet and P. caseicolum aspartyl-proteinase had a very similar action on the latter substrate, which prevented clear definition of the respective actions of these proteinases on αs1-casein after 7 d of ripening. Plasmin action on β-casein was important from 21 and 35 d of ripening at the surface and in the centre of the cheese respectively, suggesting an important influence of pH changes during maturation. The respective activities of the metallo-and aspartyl-proteinases of P. caseicolum were characterized and followed using β-casein degradation products as markers. The metallo-proteinase activity was detectable immediately after the development of the Penicillium (7 d), while that of the aspartyl-proteinase was observed 3 d later. Thereafter, the amount of β-casein degradation peptides resulting from the metalloproteinase decreased while that resulting from the aspartyl-proteinase increased, suggesting a more important role of the latter enzyme.