Hydrolysis of polyamino acids by an extracellular protease from Penicillium cyaneo-fulvum

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Abstract
The hydrolysis of polyamino-acids by an extracellular protease from P. cyaneo-fulvum was investigated. Polyaspartic-acid, polyglutamic-acid and polylysine were substrates for the enzyme, with hydrolysis occurring optimally at pH 4.3, 4.5 and 10.7 respectively. Polyproline was not a substrate. Cleavage was essentially random in nature. The initial rates of cleavage at the pH optima and 38[degree] were approximately 50, 400 and 680 mole bonds cleaved/mole of enzyme/min. for polyaspartic-acid, polyglutamic-acid and polylysine respectively. Di-, tri- and tetra-lysine are the final products of the enzymic digestion of polylysine. During hydrolysis of polylysine, there is an accumulation of intermediate peptides from the pentamer upwards. The relative rates of cleavage of penta-, hexa-and poly-lysine were approximately 1:10:140.

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