ArticleMolecular biology reports2019
Molecular cloning, expression and characterization of poxa1b gene from Pleurotus ostreatus.
Article in Molecular biology reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 15 citations in OpenAlex.
- Cloning and Heterologous Expression of Laccase from Beauveria pseudobassiana PHF4 in E. coli and its Application in the Degradation of Catechol.Current microbiology · 2026Article
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
- Green treatments for polyaromatic hydrocarbons in e-wastes.Biodegradation · 2025Review
- Molecular cloning, expression, and bioinformatics analysis of the CueO laccase gene from Escherichia coli SDB2.Molecular biology reports · 2025Article
- Identification and characterization of a novel light-induced promoter for recombinant protein production in Pleurotus ostreatus.Journal of microbiology (Seoul, Korea) · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent decades, fungus laccases (p-diphenol-dioxygen oxidoreductases; EC 1.10.3.2) have attracted the attention of researches due to their wide range of biotechnological and industrial applications. In the present study, we have cloned a gene encoding laccase (poxa1b) from Pleurotus ostreatus and then heterologously expressed in Escherichia coli BL21. The biochemical properties of POXA1b were characterized using ABTS as a typical substrate of laccases. Moreover, the in vitro oxidation of the benzo[a]pyrene was investigated in the presence or absence of ABTS. The codon-optimized poxa1b showed higher expression yields and efficiency in comparison with the wild-type (p < 0.01). The maximum activity of POXA1b (2075 UL-1) was observed after incubation at 50 °C for 0.5 h and the enzyme retained more than 85% of its initial activity after 2 h incubation at 25-45 °C. The optimum pH of the enzyme was pH4 and the enzyme was stable when being incubated at pH range from 2.5 to 4.5 for 2 h in the absence of ABTS, the enzyme oxidized a little amount of benzo[a]pyrene, whereas its oxidation enhanced following the ABTS addition. These findings indicate POXA1b of P. ostreatus as a promising candidate for further biotechnological approaches.
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