ArticleApplied microbiology and biotechnology2023
Improvement of thermoalkaliphilic laccase (CtLac) by a directed evolution and application to lignin degradation.
Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Development of SpyTag/SpyCatcher-driven thermostable cyclic laccase and its application in lignin and dye degradation and polymerization of phenolic compounds.Science China. Life sciences · 2026Article
- Advances in zearalenone-degrading enzymes research: characteristics, mining, improvement, and application.Journal of animal science and biotechnology · 2025Review
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
- Enzymatic Treatment of Lignin in Alkaline Homogeneous Systems: A Review on Alkaliphilic Laccases.ChemSusChem · 2025Review
- Deep eutectic solvents assisted laccase pretreatment for improving enzymatic hydrolysis of corn stover.Bioprocess and biosystems engineering · 2025Article
- In Vitro Fermentation of Beechwood Lignin-Carbohydrate Complexes Provides Evidence for Utilization by Gut Bacteria.Nutrients · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermoalkaliphilic laccase (CtLac) from the Caldalkalibacillus thermarum strain TA2.A1 has advantageous properties with potential industrial applications, such as high enzyme activity and stability at 70 °C and pH 8.0. In the present study, a directed evolution approach using a combination of random and site-directed mutagenesis was adopted to enhance the laccase activity of CtLac. Spectrophotometric assay and real-time oxygen measurement techniques were employed to compare and evaluate the enzyme activity among mutants. V243 was targeted for site-directed mutagenesis based on library screening. V243D showed a 25-35% higher laccase activity than wild-type CtLac in the spectrophotometric assay and oxygen consumption measurement results. V243D also showed higher catalytic efficiency than wild-type CtLac with decreased K
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