ISOLATION AND CHARACTERIZATION OF AN L-AMINO ACID ACYLASE FROM Aspergillus oryzae

Article abstract of DOI:10.1007/BF00580465

A scheme of isolating a highly purified L-amino acylase from Aspergillus oryzae is described which excludes extraction of the enzyme from the preparation "Amilorizin", fractionation with ethanol, chromatography on DEAE-cellulose, and gel filtration through Sephadex G-200 and Bio-Gel P-300.The enzyme, as purified 1240-fold, has a molecular weight of 118,000, apparently consists of two subunits with a molecular weight of 60,000, is stable in the pH range of 7-10 and has an optimum pH of 8.9 and pI of 4.0.Its amino acid composition has been determined and its substrate specificity has been studied.The acylase is a metalloenzyme: Co²⁺ ions in concentrations of 10^-4-5.10^-5 M increase the rate of hydrolysis of N-acetyl-L-amino acids three- to fourfold.It shows differences in its molecular and functional properties from acylase I obtained from porcine kidney.