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Updated: Aug 30, 2026

Single-Step Enrichment of a TAP-Tagged Histone Deacetylase of the Filamentous Fungus Aspergillus nidulans for Enzymatic Activity Assay
Published on: May 1, 2019
Crude aminoacylase from aspergillus sp. is a mixture of hydrolases
Moira L Bode1, Fred van Rantwijk, Roger A Sheldon
1Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands. BOC-Secretariat@tnw.tudelft.nl
Abstract:
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.
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