Abstract

AbstractThe formation of N‐acetyl‐β‐D‐hexosaminidase is under carbon catabolite repression in growing Penicillium chrysogenum. The enzyme accumulates inside the cells during the stationary phase of growth and is released into the culture fluid when the cell‐wall lysis has started and progressed. The time‐course of enzyme formation strongly supports the suggestion that fungal N‐acetyl‐β‐D‐hexosaminidase may have a role in the degradation of intermediate cell‐wall breakdown products during starvation. Regarding that analogous enzymes from other fungi have been shown to be able to liberate GlcNAc monomers from different glycoproteins and glycopeptides a possible participation in the orderly destruction of cellular glycoprotein components cannot be excluded. The physical and enzyme kinetic properties of both intracellular and extracellular N‐acetyl‐β‐D‐hexosaminidase are essentially the same indicating that the enzyme is probably released into the culture fluid without modification.

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