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Preventing catastrophic climate events warrants prompt action to delay global warming, which threatens health and food security. In this context, waste management using engineered microbes has emerged as a long-term eco-friendly solution for addressing the global climate crisis and transitioning to clean energy. Notably, Pseudomonas putida can valorize industry-derived synthetic wastes including plastics, oils, food, and agricultural waste into products of interest, and it has been extensively explored for establishing a fully circular bioeconomy through the conversion of waste into bio-based products, including platform chemicals (e.g., cis,cis-muconic and adipic acid) and biopolymers (e.g., medium-chain length polyhydroxyalkanoate). However, the efficiency of waste pretreatment technologies, capability of microbial cell factories, and practicability of synthetic biology tools remain low, posing a challenge to the industrial application of P. putida. The present review discusses the state-of-the-art, challenges, and future prospects for divergent biosynthesis of versatile products from waste-derived feedstocks using P. putida.
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http://dx.doi.org/10.1016/j.biortech.2023.128607 | DOI Listing |
Chembiochem
September 2025
Department of Food, Environmental and Nutritional Sciences (DeFENS), University of Milan, via Mangiagalli 25, 20133, Milan, Italy.
This study investigates the synthesis of aromatic nitriles using an evolved variant of OxdF1 (L318F/F306Y), an aldoxime dehydratase from Pseudomonas putida F1, engineered for improved catalytic efficiency toward benzaldehyde oxime. The double OxdF1 (L318F/F306Y) mutant effectively catalyzes the conversion of various benzaldoxime derivatives to the corresponding nitriles. Due to the enzyme's inherent instability, immobilized whole-cell systems are employed in a flow reactor to improve its stability and broaden its applicability, with the biotransformation of benzaldehyde oxime and 2,6-difluorobenzaldehyde oxime serving as case studies.
View Article and Find Full Text PDFFish Shellfish Immunol
September 2025
College of Marine Science and Fisheries, Jiangsu Ocean University, Lianyungang, Jiangsu 222005, China; Jiangsu Key Laboratory of Marine Genetic Resources and Breeding, Jiangsu Ocean University, Jiangsu 222005, China; Jiangsu Key Laboratory of Marine Biotechnology, Jiangsu Ocean University, Lianyunga
Turbot (Scophthalmus maximus) is one of the most widely species that boasts high economic value in the aquaculture industry. In spite of the exponential growth of aquaculture, infectious bacterial diseases have caused great economic losses in turbot industry. This study isolated and identified a strain of Pseudomonas putida, denoted as DY16, and it is a conditionally pathogenic bacterium, therefore we conducted the following research on it.
View Article and Find Full Text PDFACS Synth Biol
September 2025
Department of BioSciences, Rice University, MS-140, 6100 Main Street, Houston, Texas 77005, United States.
Microbes can be programmed to record participation in gene transfer by coding biological-recording devices into mobile DNA. Upon DNA uptake, these devices transcribe a catalytic RNA (cat-RNA) that binds to conserved sequences within ribosomal RNAs (rRNAs) and perform a trans-splicing reaction that adds a barcode to the rRNAs. Existing cat-RNA designs were generated to be broad-host range, providing no control over the organisms that were barcoded.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
September 2025
Department of Chemical and Biological Engineering, University of Colorado, Boulder, 3415 Colorado Avenue, Boulder, CO, 80303, USA.
Assembly-line enzymes carry out multistep synthesis of important metabolites by using acyl carrier proteins (ACPs) to shuttle intermediates along defined sequences of active sites. Despite longstanding interest in reprogramming these systems for metabolic engineering and biosynthetic chemistry, the mechanisms underlying their reaction order remain poorly understood and difficult to control. Here we describe a β-ketoacyl-ACP reductase from Pseudomonas putida (PpFabG4) with an unusual selectivity for medium chains and use it to explore the molecular basis of substrate specificity in enzymes that pull intermediates from fatty acid synthesis, a common route to specialized products.
View Article and Find Full Text PDFCommun Biol
August 2025
Institute of Marine Science and Technology, Shandong University, Qingdao, China.
The secretion of ligninolytic enzyme provides a competitive advantage for microbial survival. These enzymes are commonly transported to the extracellular milieu via signal peptides for the catabolism of lignin, which cannot be translocated through the cell membrane. However, some bacterial ligninolytic enzymes lack signal peptides, yet they can still be secreted.
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