1. Carbobenzoxy-L-glutamyl-L-tyrosine and benzoyl-L-argininamide are readily hydrolyzed by the acid-protease of Paecilomyces varioti Bainier TPR-220, as acid-proteases of Aspergillus oryzae by Nunokawa and Asp. saitoi by Yoshida did. But the present enzyme can not hydrolyze alanylglycylglycine and leucylglycylglycine which are hydrolyzed by the above two enzymes.
2. The enzyme is optimally active at pH 3.5 and 5.5 toward carbobenzoxy-L-glutamyl-L-tyrosine and benzoyl-L-argininamide at 45°C respectively. These values of optimum pH, however, are different from that obtained from Asp. saitoi protease.
3. The hydrolysis velocity constant, Michaelis constant, and activation energy in the hydrolysis of both substrates by the enzyme were determined.

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