Toxic heavy metal accumulation is one of anthropogenic environmental pollutions, which poses risks to human health and ecological systems. Conventional heavy metal remediation approaches rely on expensive chemical and physical processes leading to the formation and release of other toxic waste products. Instead, microbial bioremediation has gained interest as a promising and cost-effective alternative to conventional methods, but the genetic complexity of microorganisms and the lack of appropriate genetic engineering technologies have impeded the development of bioremediating microorganisms. Recently, the emerging synthetic biology opened a new avenue for microbial bioremediation research and development by addressing the challenges and providing novel tools for constructing bacteria with enhanced capabilities: rapid detection and degradation of heavy metals while enhanced tolerance to toxic heavy metals. Moreover, synthetic biology also offers new technologies to meet biosafety regulations since genetically modified microorganisms may disrupt natural ecosystems. In this review, we introduce the use of microorganisms developed based on synthetic biology technologies for the detection and detoxification of heavy metals. Additionally, this review explores the technical strategies developed to overcome the biosafety requirements associated with the use of genetically modified microorganisms.
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http://dx.doi.org/10.3389/fbioe.2023.1178680 | DOI Listing |
Sci Rep
January 2025
Molecular Biology and Tissue Culture Laboratory, Department of Tea Science, University of North Bengal, Siliguri, West Bengal, India.
Several recent investigations into montane regions have reported on excess mercury accumulation in high-altitude forest ecosystems. This study explored the Singalila National Park, located on the Singalila ridge of the Eastern Himalayas, revealing substantial mercury contamination. Particular focus was on Sandakphu (3636 m), the highest peak in West Bengal, India.
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January 2025
Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Ubon Ratchathani University, Ubon Ratchathani, 34190, Thailand.
Carcinoembryonic antigen (CEA) and C-reactive protein (CRP) are biomacromolecules known as cancer and inflammatory markers. Thus, they play a crucial role in early cancer diagnosis, post-treatment recurrence detection, and tumor risk assessment. This paper describes the development of an ultrasensitive and selective imprinted paper-based analytical device (PAD) as impedance sensor for determination of CEA and CRP in serum samples for point-of-care testing (POCT).
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January 2025
Hydrobiology Lab, National Institute of Oceanography and Fisheries (NIOF), Cairo, Egypt.
The utilization of cyanobacteria toxin-producing blooms for metal ions adsorption has garnered significant attention over the last decade. This study investigates the efficacy of dead cells from Microcystis aeruginosa blooms, collected from agricultural drainage water reservoir, in removing of cadmium, lead, and zinc ions from aqueous solutions, and simultaneously addressing the mitigation of toxin-producing M. aeruginosa bloom.
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January 2025
Institute of Field and Vegetable Crops, National Institute of the Republic of Serbia, Maxim Gorki, 30, Novi Sad, 21000, Serbia.
Wheat (Triticum aestivum L.) productivity and quality can be threatened by soil cadmium (Cd) contamination, posing a concern to food security. Salicylic acid (SA) is an endogenously produced signaling molecule that activates the defense system imparting abiotic stress tolerance in plants.
View Article and Find Full Text PDFNat Commun
January 2025
Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
The mycobacterial ABC transporter IrtAB features an ABC exporter fold, yet it imports iron-charged siderophores called mycobactins. Here, we present extensive cryo-EM analyses and DEER measurements, revealing that IrtAB alternates between an inward-facing and an outward-occluded conformation, but does not sample an outward-facing conformation. When IrtAB is locked in its outward-occluded conformation in nanodiscs, mycobactin is bound in the middle of the lipid bilayer at a membrane-facing crevice opening at the heterodimeric interface.
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