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Antibiotics play a crucial role in human and animal medical healthcare, but widespread use and overuse of antibiotics poses alarming health and environmental issues. Fluoroquinolones constitute a class of antibiotics that has already become ubiquitous in the environment, and their increasing use and high persistence prompt growing concern. Here we investigated a fungal secretome prepared from the white-rot fungus , which is able to effectively degrade the environmentally persistent fluoroquinolone, levofloxacin. We tested various physical-chemical factors such as concentrations of 1-hydroxybenzotriazol (HBT), of enzyme, and of antibiotic, and pH and temperature of the reaction for biotransformation of the antibiotic. We compared the free with the immobilized secretome proteins, and analyzed the collective reaction products for residual activity against (growth inhibition test). We also performed HPLC analysis. The results show that treatment with the free secretome yielded a highest removal efficiency of 50 mg L levofloxacin in the presence of 2.5 mM HBT, whereas the immobilized secretome was only able to degrade 10 mg L levofloxacin with the same concentration of mediator, but presenting the advantage of being reusable.
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http://dx.doi.org/10.3390/jof10120861 | DOI Listing |
J Fungi (Basel)
December 2024
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, Ecole Nationale d'Ingénieurs de Sfax, Université de Sfax, Sfax 3038, Tunisia.
Antibiotics play a crucial role in human and animal medical healthcare, but widespread use and overuse of antibiotics poses alarming health and environmental issues. Fluoroquinolones constitute a class of antibiotics that has already become ubiquitous in the environment, and their increasing use and high persistence prompt growing concern. Here we investigated a fungal secretome prepared from the white-rot fungus , which is able to effectively degrade the environmentally persistent fluoroquinolone, levofloxacin.
View Article and Find Full Text PDFACS Appl Bio Mater
September 2024
Department of Chemical and Petroleum Engineering, University of Calgary, 2500 University Drive NW, Calgary, Alberta T2N 1N4, Canada.
J Proteome Res
December 2023
Centre for Proteome Research, Institute of Systems, Molecular & Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalyzed by Golgi-resident tyrosyl protein sulfo transferases (TPSTs). Information on sY in humans is currently limited to ∼50 proteins, with only a handful having verified sites of sulfation. As such, the contribution of sulfation to the regulation of biological processes remains poorly defined.
View Article and Find Full Text PDFBiosens Bioelectron
August 2023
Department of Immunology, State Research Institute Centre for Innovative Medicine, LT-08406, Vilnius, Lithuania; NanoTechnas ‒ Center of Nanotechnology and Materials Science, Institute of Chemistry, Faculty of Chemistry and Geosciences, Vilnius University, LT-03225, Vilnius, Lithuania.
This paper reports the development of a novel surface plasmon resonance (SPR) immunosensor for ultra-sensitive quantitative determination of human articular cartilage oligomeric matrix protein (COMP), a major component of the extracellular matrix and an exploratory biomarker. Capture antibodies against human COMP (anti-COMP) were covalently immobilized on an 11-mercaptoundecanoic acid (11-MUA) self-assembled monolayer (SAM)-coated SPR sensor disk and a dual sandwich-type signal amplification strategy using biotinylated detection antibodies against COMP (anti-COMP) and streptavidin-conjugated quantum dots (SAv‒QDs) were used for the development of an immunosensor. The binding of high-mass SAv‒QDs via biotin-streptavidin interaction to the surface of the immunosensor resulted in a drastic increase in the sensitivity.
View Article and Find Full Text PDFPhysiol Genomics
August 2022
Department of Cellular Biology and Anatomy, Medical College of Georgia at Augusta University, Augusta, Georgia.
Fibro-adipogenic progenitor cells (FAPs) are a population of stem cells in skeletal muscle that play multiple roles in muscle repair and regeneration through their complex secretome; however, it is not well understood how the FAP secretome is altered with muscle disuse atrophy. Previous work suggests that the inflammatory cytokine IL-1β is increased in FAPs with disuse and denervation. Inflammasome activation and IL-1β secretion are also known to stimulate the release of extracellular vesicles (EVs).
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