Abstract
A proteolytic enzyme from culture fluids of Aspergillus oryzae was purified by a multistep procedure including carrier-free electrophoresis and DEAE-Sephadex chromatography. It was a homogenous protein, judging from results obtained by disc electrophoresis, immunoelectrophoresis and end-group determination. The enzyme hydrolysed native collagen at a slow rate. Electron microscopic investigations of the digest revealed triple-helical fragments remaining after degradation of the collagen molecule at its N-terminal end. The results thus contribute to a current discussion on collagenolysis by proteolytic enzymes other than specific collagenases.
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