ArticleMolecular biotechnology2016
In-Vitro Refolding and Characterization of Recombinant Laccase (CotA) From Bacillus pumilus MK001 and Its Potential for Phenolics Degradation.
Article in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- Bacterial laccases for green remediation of contaminants of emerging concern: from molecular cloning to metagenomic and computational insights.Biodegradation · 2026Review
- Improvement of aflatoxin BHeliyon · 2023Article
- Structure/epitope analysis and IgE binding activities of three cyclophilin family proteins from Dermatophagoides pteronyssinus.Scientific reports · 2023Article
- An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency.International journal of molecular sciences · 2023Article
- Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.Microbial biotechnology · 2021Article
- Manganese Stress Adaptation Mechanisms ofFrontiers in microbiology · 2021Article
- Degradation of Aflatoxin BToxins · 2019Article
- Bacterial laccases: promising biological green tools for industrial applications.Cellular and molecular life sciences : CMLS · 2018Review
- Functional Expression of a Thermostable Endoglucanase from Thermoascus aurantiacus RCKK in Pichia pastoris X-33 and Its Characterization.Molecular biotechnology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among lignocellulolytic enzymes, laccases are the most versatile, broadly specific, and largely studied enzyme with a wide range of biotechnological potential. Putative laccase (CotA) from Bacillus pumilus MK001 was cloned and expressed in E. coli. In addition to soluble bioactive fraction, inactive inclusion body fraction was also harvested and refolded under optimized conditions resulting in 64 % of refolding efficiency. The enzyme was found to be thermostable exhibiting a half-life of 60 min at 80 °C. UV thermal CD spectra also supported the observation as about 9 % increase in β-sheets was recorded after thermal induction. The 3D CotA structure was constructed through homology modeling and the best selected model was verified through PROCHECK, ERRAT, Verify 3D, and PROSA servers. Final 3D model showed potential binding affinities with ferulic acid, caffeic acid, and vanillin. Results of the docking studies were further validated by HPLC analysis which signified the efficient bioconversion ability of CotA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.