Chitin synthase activity was detected in actively growing mycelium of after mechanical disruption of the cells. Chitin formation in fungal extracts at 32 ° was linear with respect to time for at least 60 min, and with respect to protein concentration up to 750 μg ml. The optimum pH for enzyme activity was 8.5 using 10 m-Tris/HC1 buffer. Mg was necessary for maximum activity and 10 m-MgC1 was routinely used during the assays. The apparent for the substrate UDP-GlcNAc was 2 m. Polyoxin D was a competitive inhibitor of chitin synthesis with an apparent of 4 μ. Following treatment with trypsin (12.5 μg ml), the chitin synthase activity of the fungal extract increased by six-fold, indicating that most of the chitin synthase activity was zymogenic. The reaction product was insoluble in 1 -KOH or 1 -acetic acid, but it was solubilized by heating in 6 -HC1 at 120 ° for 2.5 h and was hydrolysed by chitinase into diacetylchitobiose.


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