Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 61, Issue 3-4, Pages 261-267Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2009.08.004
Keywords
Laccase inhibitor; Laccase assay; White rot fungi; Trametes villosa; Carboxylic acid
Funding
- Competence Center
- Austrian Government
- Upper Austria, Lower Austria, and Carinthia
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The inhibition of fungal laccases by carboxylic acids has been studied. Steady-state kinetics performed with recombinant laccase from Trametes villosa and ABTS as a substrate revealed an s-linear, i-parabolic mixed inhibition type for acetate, while formate exhibited a linear, non-competitive inhibition type. Although Ki values were several orders of magnitude higher than those for azide, inhibition levels for acetate were substantial (10-60% of initial activity) at concentrations commonly used in routine laccase assays (10-100 mM). The first order inactivation rate constant for acetate was low (0.39 min(-1)) and similar to that of propionate and butyrate. However, inhibition by di- and tricarboxylic acids was considerably less pronounced (up to 20% at 100 mM) and instantaneous. Therefore. citrate and particularly succinate appear much more suitable for laccase assays and applications than acetate which should be avoided. Wild-type laccases from several Trametes species were found to be inhibited to a similar extent, while laccase from Pleurotus eryngii and some other species were not affected or even stimulated by carboxylic acids. These results collectively suggest that fungal laccases do not share a common structural feature responsible for their inhibition by carboxylic acids. (C) 2009 Elsevier B.V. All rights reserved.
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