Protease inhibitor activity is associated to a basic chitinase from potato but not to an acidic one

Several pathogenesis-related proteins, which are produced in plants submitted to stress, have been identified as chitinases. We have previously described that a potato basic chitinase strongly inhibited the activity of an aspartic protease isolated from the same source. In this work, we have tested the activity of two potato chitinases as protease inhibitors. A basic chitinase (ChiB) inhibited trypsin, chymotrypsin, subtilisin, proteinase K and a serine protease of Fusarium sp. An acidic one (ChiA) did not show inhibitory activity. The kinetics of trypsin inhibition by ChiB revealed different patterns of inhibition with azocasein and BAPNA. Metal ions affected differentially both activities, suggesting that ChiB is a bifunctional protein. These results and those reported by other authors suggest a new physiological role for pathogenesis-related proteins. However, results presented in this paper suggest that the protease inhibitor activity is not a general characteristic of potato chitinases.