| Abstract | Two proteases isolated from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) had different isoelectric points but similar pH optimums. The components were inhibited by equal amounts of ovomucoid. Heat studies showed that the constituent moving towards the cathode (cathodic component) was more stable at 58 °C. than the anodic component. The enzyme located in the cathodic component hydrolzyed chloroacetyl-L-tyrosine. The same fraction also hydrolyzed N-carbobenzoxy-α-L-glutamyl-DL-alanine and to a much lesser extent N-carbobenzoxy-α-L-glutamyl-L-glutamic acid. No enzymatic activity could be detected against glycylglycine, diglycylglycine, glycyl-L-proline, seryl-serine, or α-benzoyl-L-argininamide. |
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