The enzymatic properties of the water-insoluble aminoacylase prepared by linking mold aminoacylase (EC 3. 5. 1. 14) to DEAE-Sephadex were studied and compared with those of the native aminoacylase.
Optimum pH values for hydrolysis of several substrates by the DEAE-Sephadex-amino-acylase complex (DSA-complex) shifted about 0.5_??_1.5 pH units more to the acid side than those by the native enzyme. On the effects of metal ions and inhibitors, substrate specificity, optical specificity and kinetic constants, no marked difference was observed between the native enzyme and the DSA-complex. Heat stability, optimum temperature and resistance towards proteases were increased by conversion from the native form to the insoluble enzyme. It was also observed that the DSA-complex was activated by urea.

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