Benzophenone-3 (2-hydroxy-4-methoxybenzophenone, BP-3) poses risks to human health and natural ecosystems, and means to improve its biodegradation are necessary. When a small mass of Rhodococcus ruber, isolated from BP-3-acclimated biomass, was bioaugmented into the acclimated biomass, BP-3 removal was accelerated by 120 %. The first step of BP-3 biodegradation generates either 2,5-dihydroxy-4-methoxybenzophenone (5-OH-BP-3) or benzophenone-1 (2,4-dihydoxybenzophenone, BP-1). BP-1 is generated by sequential demethylation, hydroxylation, and dehydrogenation reactions, while 5-OH-BP-3 is generated by one mono-oxygenation reaction. Of the two intermediates, 5-OH-BP-3 exhibited stronger inhibition than BP-1 or the original BP-3. Gene-completion mapping showed that R. ruber contains genes for demethylase, hydrolase, dehydrogenase, and mono-oxygenase reaction, which means that R. ruber could generate the less-toxic BP-1. Thus, bioaugmentation of R. ruber into BP-3-acclimated biomass eliminated the accumulation of 5-OH-BP-3 and, consequently, accelerated of BP-3 biodegradation via BP-1.
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http://dx.doi.org/10.1016/j.jhazmat.2024.136566 | DOI Listing |
J Hazard Mater
January 2025
Biodesign Swette Center for Environmental Biotechnology, Arizona State University, Tempe, AZ 85287-5701, USA.
Benzophenone-3 (2-hydroxy-4-methoxybenzophenone, BP-3) poses risks to human health and natural ecosystems, and means to improve its biodegradation are necessary. When a small mass of Rhodococcus ruber, isolated from BP-3-acclimated biomass, was bioaugmented into the acclimated biomass, BP-3 removal was accelerated by 120 %. The first step of BP-3 biodegradation generates either 2,5-dihydroxy-4-methoxybenzophenone (5-OH-BP-3) or benzophenone-1 (2,4-dihydoxybenzophenone, BP-1).
View Article and Find Full Text PDFHeliyon
November 2024
Department of Microbiology, Federal University of Viçosa, Viçosa, Minas Gerais, Brazil.
Front Chem
August 2024
Faculty of Food technology and Biotechnology, University of Zagreb, Zagreb, Croatia.
Stabilized enzymes are crucial for the industrial application of biocatalysis due to their enhanced operational stability, which leads to prolonged enzyme activity, cost-efficiency and consequently scalability of biocatalytic processes. Over the past decade, numerous studies have demonstrated that deep eutectic solvents (DES) are excellent enzyme stabilizers. However, the search for an optimal DES has primarily relied on trial-and-error methods, lacking systematic exploration of DES structure-activity relationships.
View Article and Find Full Text PDFAppl Environ Microbiol
August 2024
Department of Chemical and Biomolecular Engineering, Rice University, Houston, Texas, USA.
Soil-dwelling Actinomycetes are a diverse and ubiquitous component of the global microbiome but largely lack genetic tools comparable to those available in model species such as or , posing a fundamental barrier to their characterization and utilization as hosts for biotechnology. To address this, we have developed a modular plasmid assembly framework, along with a series of genetic control elements for the previously genetically intractable Gram-positive environmental isolate C208, and demonstrate conserved functionality in 11 additional environmental isolates of , , and . This toolkit encompasses five Mycobacteriale origins of replication, five broad-host-range antibiotic resistance markers, transcriptional and translational control elements, fluorescent reporters, a tetracycline-inducible system, and a counter-selectable marker.
View Article and Find Full Text PDFMol Biol Rep
July 2024
Key Laboratory of Industrial Biocatalysis, Ministry of Education, Beijing, China.
Background: Nitrile Hydratase (NHase) is one of the most important industrial enzyme widely used in the petroleum exploitation field. The enzyme, composed of two unrelated α- and β-subunits, catalyzes the conversion of acrylonitrile to acrylamide, releasing a significant amount of heat and generating the organic solvent product, acrylamide. Both the heat and acrylamide solvent have an impact on the structural stability of NHase and its catalytic activity.
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