Purification and Properties of Leucine Aminopeptidase IV from Aspergillus oryzae

Abstract

Leucine aminopeptidase IV in extracts of wheat bran culture of Aspergillus oryzae 460 was separated from arylamidase by polyacrylamide gel disc electrophoresis at pH 8.0 for 1 hr. The purified enzyme showed neither arylamidase nor amidase activity. The optimum pH was 7.0 on L-leucyl-L-glycyl-L-glycine (Leu-Gly-Gly) as substrate. The enzyme wasinhibited by diisopropylphosphorofluoridate (DFP), but not by metal chelating agents. The enzyme molecular weight was estimated to be about 130,000 by gel filtration method. © 1977, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.