2004
DOI: 10.1016/j.biochi.2004.07.013
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Tannic acid interferes with the commonly used laccase-detection assay based on ABTS as the substrate

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Cited by 26 publications
(17 citation statements)
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“…A radical cation (ABTS + ) was created during the oxidation of ABTS by laccase [24]. This green-blue colored cation was determined using a Jasco V650 spectrophotometer by measuring the absorbance at 420 nm.…”
Section: Laccase Activity Assaymentioning
confidence: 99%
“…A radical cation (ABTS + ) was created during the oxidation of ABTS by laccase [24]. This green-blue colored cation was determined using a Jasco V650 spectrophotometer by measuring the absorbance at 420 nm.…”
Section: Laccase Activity Assaymentioning
confidence: 99%
“…We therefore ensured the production of such fungal laccase by non-denaturing PAGE analysis using ABTS as a substrate, which turned green upon the enzyme-catalyzed oxidation ( Supplementary Fig. S4) 17 . The genomic data ascertained a laccase-encoding gene lacTL existing at the directly downstream locus of pksTL (GenBank Nucleotide Core accession code: JX025148).…”
Section: Discussionmentioning
confidence: 99%
“…Correlating to the capability of a fungal laccase catalyzing the coupling reaction of phenolic molecules 16 , we hypothesized that the fungus could have produced laccase(s) capable of catalyzing the C-C bondage among naphthol motifs to give the corresponding enantiomeric mixtures. Using the protocol detailed elsewhere 17 , the presence of laccase in the fungal protein was ensured by the non-denaturing polyacrylamide gel electrophoresis (PAGE) analysis utilizing the substrate ABTS (2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate)), which gave characteristically the green band upon the oxidation catalyzed by the enzyme (Supplementary Fig. S4).…”
Section: Confirmation Of Naphthol Residues As Building Blocksmentioning
confidence: 99%
“…Therefore, determination of laccase activity in the presence of catalase (to remove H 2 O 2 ) and ethylenediaminetetraacetic acid (EDTA; for chelating of the Mn 2+ needed for MnP activity) using a typical substrate of ABTS is an efficient assay method for laccases . However, it has been reported that the molar extinction coefficient ( ε ) of ABTS strongly depends on the origin of the laccases and the exact assay conditions . For example, Zimmermann et al reported that the molar extinct coefficient is 36,000 M/cm at pH 3 while Ander and Messner estimated an extinction coefficient of 43,200 M/cm at pH 4.5.…”
Section: Determination Of Laccase Activitymentioning
confidence: 99%
“…For example, Zimmermann et al reported that the molar extinct coefficient is 36,000 M/cm at pH 3 while Ander and Messner estimated an extinction coefficient of 43,200 M/cm at pH 4.5. Furthermore, the radical cation ABTS +• produced by laccase oxidation can be reduced to ABTS by several organic compounds, such as tannic acid, which thus shows a false decrease in laccase activity . Terron et al showed that the characteristic shoulder at 420 nm of ABTS was completely abolished in the presence of tannic acid (>0.5 μM).…”
Section: Determination Of Laccase Activitymentioning
confidence: 99%