Abstract
Ch3, an endochitinase of 32 kDa present in Castanea sativa cotyledons, showed in vitro antifungal properties when assayed against Trichoderma viride. The characterization of a cDNA clone corresponding to this protein indicated that Ch3 is a class Ib endochitinase that is synthesized as a preprotein with a signal sequence preceding the mature polypeptide. Bacterial expression of mature Ch3 fused to the leader peptide of the periplasmic protein ompT resulted in active Ch3 enzyme. A plate assay was adapted for semi-quantitative determination of chitinase activity secreted from cultured bacteria, which should facilitate the identification of mutants with altered capacity to hydrolyse chitin.
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Allona, I., Collada, C., Casado, R. et al. Bacterial expression of an active class Ib chitinase from Castanea sativa cotyledons. Plant Mol Biol 32, 1171–1176 (1996). https://doi.org/10.1007/BF00041402
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DOI: https://doi.org/10.1007/BF00041402