ArticleJournal, genetic engineering & biotechnology2022
2,4-Dichlorophenol biotransformation using immobilized marine halophilic Bacillus subtilis culture and laccase enzyme: application in wastewater treatment.
Article in Journal, genetic engineering & biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 13 citations in OpenAlex.
- Optimizing fermentation conditions for enhanced laccase production from Coriolus versicolor and its potential in degrading 2,4-dichlorophenol.Bioprocess and biosystems engineering · 2025Article
- Review of research progress in immobilization and chemical modification of microbial enzymes and their application.Microbial cell factories · 2025Review
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3 authors at 2 institutions in 1 country.
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Abstract
background2,4-Dichlorophenol (2,4-DCP) is a very toxic aromatic compound for humans and the environment and is highly resistant to degradation. Therefore, it is necessary to develop efficient remediation and cost-effective approaches to this pollutant. Microbial enzymes such as laccases can degrade phenols, but limited information is known about immobilized bacterial laccase and their reuse.
methodsImmobilization of marine halophilic Bacillus subtilis AAK cultures via entrapment and adsorption techniques and degradation of different phenolic compounds by immobilized cells were estimated. Partial purification and immobilization of laccase enzymes were carried out. In addition, the biodegradation of 2,4-DCP and others contaminated by wastewater was investigated.
resultsImmobilization of cells and partially purified laccase enzymes by adsorption into 3% alginate increased 2,4-DCP biotransformation compared with free cells and free enzymes. In addition, the reuse of both the immobilized culture and laccase enzymes was evaluated. The highest removal of 2,4-DCP from pulp and paper wastewater samples inoculated by immobilized cells and the immobilized enzyme was 90% and 95%, respectively, at 50 h and 52 h of incubation, compared to free cells and free enzyme.
conclusionThe results of this study have revealed the immobilization of a biocatalyst and its laccase enzyme as a promising technique for enhancing the degradation of 2,4-DCP and other toxic phenolic and aromatic compounds. The reuse of the biocatalyst and its laccase enzyme enabled the application of this cost-effective bioremediation strategy.
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