Comparative Studies of the Enzymatic Properties of Novo and Carlsberg Subtilisins

The activities of Carlsberg and Novo subtilisins towards a number of N-acetylamino acid esters and amino acid esters have been examined. The enzymes were also compared with respect to their efficiency in catalyzing aminolysis reactions, their rates of inactivation by certain aromatic sulfonyl halides, and the rates of deacylation of their N-trans-cinnamoyl derivatives. The enzymes were found to be qualitatively indistinguishable from the standpoint of substrate specificity. However, significant quantitative differences were observed. The results obtained suggest that the substrate-binding site of Carlsberg subtilisin is less polar than that of the Novo enzyme, and that the groups in the catalytic site of Carlsberg subtilisin show a somewhat higher reactivity than the corresponding groups in Novo subtilisin.