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'Aspergillus Am inoacylase' in keywords Facet   Publication Year 1980  [X]
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1980[X]
1Author    Ingrid Gentzen, Hans-G Löffler, Friedh SchneiderRequires cookie*
 Title    Aminoacylase from Aspergillus oryzae. Comparison with the Pig Kidney Enzyme  
 Abstract    Am inoacylase (EC 3.5.1.14) from Aspergillus oryzae was purified from a com m ercially available crude material by heat treatment, precipitation by polyethyleneim ine and amm onium sulfate, gel chromatography and preparative disc-gel-electrophoresis. The purified product was hom ogenous as judged by polyacrylamide gel electrophoresis. SDS-gel electrophoresis, polyacrylam ide-gel-gradient electrophoresis, gel chromatography and amino acid analysis demonstrated the enzyme to be com posed o f two subunits with M r o f 36 600. The kinetic properties o f the enzyme were studied with chloroacetyl derivatives o f alanine, phenylalanine, methionine, leucine, norleucine and tryptophan. The pH optim um o f the acylase activity with chloroacetyl-alanine as substrate is at pH 8.5. Acyl derivatives o f hydrophobic am ino acids are preferred substrates. The enzyme has no dipeptidase activity. Am inoacylase is not inhibited by SH -blocking agents and no SH-groups could be detected with Ellman's reagent in the native and denatured enzyme. The enzyme activity is insensitive to phenylmethylsulfonyl fluoride and N-a-/?-tosyl-L-lysine chlorom ethyl ketone. The microbial acylase is a zinc m etallo enzyme. M etal chelating agents are strong inhibitors; it is further inhibited by Cd2+, Mn2+, N i2+, C u2+ and activated by C o2+. The properties o f pig kidney and Aspergillus acylase are compared. 
  Reference    Z. Naturforsch. 35c, 544 (1980); received February 21 1980 
  Published    1980 
  Keywords    Aspergillus Am inoacylase, Purification, Properties 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0544.pdf 
 Identifier    ZNC-1980-35c-0544 
 Volume    35