ArticleScientific reports2018
Multiple Reaction Monitoring for quantitative laccase kinetics by LC-MS.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 35 citations in OpenAlex.
- Comparative Characterization of Oxidative Enzymes for Arabinoxylan and Protein Cross-Linking via Ferulic Acid and Tyrosine in Model Systems.Journal of agricultural and food chemistry · 2025Article
- Selective and green conversion of 5-HMF to FDCARSC advances · 2025Article
- Laccase-Mediated Incorporation of Xylans and Lignin-Carbohydrate Complexes into High-Yield Eucalyptus Kraft Fibers.ACS omega · 2025Article
- Microbiological Aspects and Enzymatic Characterization ofJournal of fungi (Basel, Switzerland) · 2024Article
- Effects of Lignin-Diverted Reductant with Polyphenol Oxidases on Cellulose Degradation by Wild and Mutant Types of Lytic Polysaccharide Monooxygenase.Current issues in molecular biology · 2024Article
- Isolation and test of novel yeast strains with lignin usage capability and phenolic compound resistance.MicrobiologyOpen · 2022Article
- Isothermal titration calorimetric assessment of lignin conversion by laccases.Biotechnology and bioengineering · 2022Article
- Substrate Specificity of LACCASE8 Facilitates Polymerization of Caffeyl Alcohol for C-Lignin Biosynthesis in the Seed Coat ofThe Plant cell · 2020Article
- Article
- A structural-chemical explanation of fungal laccase activity.Scientific reports · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccases (EC 1.10.3.2) are enzymes known for their ability to catalyse the oxidation of phenolic compounds using molecular oxygen as the final electron acceptor. Lignin is a natural phenylpropanoids biopolymer whose degradation in nature is thought to be aided by enzymatic oxidation by laccases. Laccase activity is often measured spectrophotometrically on compounds such as syringaldazine and ABTS which poorly relate to lignin. We employed natural phenolic hydroxycinnamates having different degree of methoxylations, p-coumaric, ferulic and sinapic acid, and a lignin model OH-dilignol compound as substrates to assess enzyme kinetics by HPLC-MS on two fungal laccases Trametes versicolor laccase, Tv and Ganoderma lucidum laccase, Gl. The method allowed accurate kinetic measurements and detailed insight into the product profiles of both laccases. Both Tv and Gl laccase are active on the hydroxycinnammates and show a preference for substrate with methoxylations. Product profiles were dominated by the presence of dimeric and trimeric species already after 10 minutes of reaction and similar profiles were obtained with the two laccases. This new HPLC-MS method is highly suitable and accurate as a new method for assaying laccase activity on genuine phenolic substrates, as well as a tool for examining laccase oxidation product profiles.
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