Crude aminoacylase from aspergillus sp. is a mixture of hydrolases.
A range of cross-linked enzyme aggregates (CLEAs) was prepared from commercially available aminoacylase I. Results from three test reactions showed that aminoacylase does not possess aminolysis or alcoholysis activity, both previously ascribed to this enzyme. This result was confirmed using aminoacylase purified by chromatographic techniques, which leads us to conclude that the previously observed acylations of esters and amines is due to other enzymes present as impurities in the crude aminoacylase I.
Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands. BOC-Secretariat@tnw.tudelft.nl
Moira L
ML
Bode
Fred
F
van Rantwijk
Roger A
RA
Sheldon
D000215:Acylation; D000581:Amidohydrolases / Q000737:chemistry* / Q000145:classification* / Q000302:isolation & purification; D001230:Aspergillus / Q000201:enzymology*; D045424:Complex Mixtures / Q000737:chemistry* / Q000145:classification* / Q000302:isolation & purification; D003432:Cross-Linking Reagents / Q000737:chemistry; D006867:Hydrolases / Q000737:chemistry* / Q000145:classification* / Q000302:isolation & purification; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000302:isolation & purification
D045424:Complex Mixtures; D003432:Cross-Linking Reagents; D007527:Isoenzymes; D006867:Hydrolases; D000581:Amidohydrolases; C019672:aminoacylase I