ArticleBMC biotechnology2021
Recombinant laccase rPOXA 1B real-time, accelerated and molecular dynamics stability study.
Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Class-Specific Immunochromatographic Assay Enabled by Mesoporous Nanozyme-Catalyzed Signal Amplification for On-Site Screening of Sulfonylureas.Foods (Basel, Switzerland) · 2026Article
- Machine learning for enzyme catalytic activity: current progress and future horizons.Briefings in bioinformatics · 2026Review
- Storage stability of lysostaphin solution and its pulmonary delivery.Drug delivery and translational research · 2024Article
- Statistical Improvement of rGILCC 1 and rPOXA 1B Laccases Activity Assay Conditions Supported by Molecular Dynamics.Molecules (Basel, Switzerland) · 2023Article
- Impact of Antibiotics as Waste, Physical, Chemical, and Enzymatical Degradation: Use of Laccases.Molecules (Basel, Switzerland) · 2022Review
- D-Mannoside FimH Inhibitors as Non-Antibiotic Alternatives for UropathogenicAntibiotics (Basel, Switzerland) · 2021Article
- A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases.Molecules (Basel, Switzerland) · 2021Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLaccases (EC 1.10.3.2) are multi-copper oxidoreductases with great biotechnological importance due to their high oxidative potential and utility for removing synthetic dyes, oxidizing phenolic compounds, and degrading pesticides, among others.
methodsA real-time stability study (RTS) was conducted for a year, by using enzyme concentrates from 3 batches (L1, L3, and L4). For which, five temperatures 243.15, 277.15, 298.15, 303.15, 308.15, and 313.15 K were assayed. Using RTS data and the Arrhenius equation, we calculated the rPOXA 1B accelerated stability (AS). Molecular dynamics (MD) computational study results were very close to those obtained experimentally at four different temperatures 241, 278, 298, and 314 K.
resultsIn the RTS, 101.16, 115.81, 75.23, 46.09, 5.81, and 4.83% of the relative enzyme activity were recovered, at respective assayed temperatures. AS study, showed that rPOXA 1B is stable at 240.98 ± 5.38, 277.40 ± 1.32 or 297.53 ± 3.88 K; with t
conclusionsLaccase rPOXA 1B demonstrated experimentally and computationally to be a stable enzyme, with t
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