Pharmaceutical studies on aminopeptidase from Aspergillus japonica. I.

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Abstract
To utilize aminopeptidase from A. japonica as a digestive enzyme preparation, the properties of the crude enzyme were examined from pharmaceutical aspects. The enzyme was most active at pH 8.0 and 50.degree. C, and was stable in a pH range of 5.5 to 8.5 and below 50.degree. C. The enzyme was activated by Co2+, but was strongly inhibited by some metal ions, o-phenanthroline, and N-bromosuccinimide. Hydrolytic cross-reaction between the enzyme and various proteases was carried out using casein as a substrate. The hydrolysis ratio (60%) was 2-fold greater than that by only the individual proteases. The enzyme is considered to be useful for digesting a protein, together with other proteases. From the examination of the stability of the enzyme powder and that of the enzyme to various pharmaceutical factors, the enzyme was found to be highly stable to diluents, binders, and wetting agents at a high concentration, and was also stable to low first pressure in tabletting. It is suggested that this aminopeptidase can be satisfactorily utilized as a digestive enzyme preparation.

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