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Recently, bio-based manufacturing processes of value-added platform chemicals and polymers in biorefineries using renewable resources have extensively been developed for sustainable and carbon dioxide (CO) neutral-based industry. Among them, bio-based diamines, aminocarboxylic acids, and diacids have been used as monomers for the synthesis of polyamides having different carbon numbers and ubiquitous and versatile industrial polymers and also as precursors for further chemical and biological processes to afford valuable chemicals. Until now, these platform bio-chemicals have successfully been produced by biorefinery processes employing enzymes and/or microbial host strains as main catalysts. In this review, we discuss recent advances in bio-based production of diamines, aminocarboxylic acids, and diacids, which has been developed and improved by systems metabolic engineering strategies of microbial consortia and optimization of microbial conversion processes including whole cell bioconversion and direct fermentative production.
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http://dx.doi.org/10.1016/j.biotechadv.2022.108070 | DOI Listing |
Environ Sci Technol
July 2025
State Key Laboratory of Urban Water Resource and Environment, School of Environment, Harbin Institute of Technology, Harbin 150090, China.
Research promoting the use of aminocarboxylate ligands to enhance metal ion oxidation of pollutants in advanced oxidation processes (AOPs) has gained increasing interest in recent years. In this work, the most common ligand, ethylenediaminetetraacetic acid (EDTA), was used to enhance Mn(II) activation of periodate (PI, IO) for the degradation of the sulfisoxazole (SIZ). Chromatographic analysis of EDTA showed that EDTA, like SIZ, also exhibits self-accelerated degradation in this system.
View Article and Find Full Text PDFBiotechnol Adv
December 2022
Department of Chemical Engineering and Materials Science, Graduate Program in System Health Science and Engineering, Ewha Womans University, 52 Ewhayeodae-gil, Seodaemun-gu, Seoul 03760, Republic of Korea. Electronic address:
Chem Commun (Camb)
March 2020
Biological Chemistry Group, Institute of Biology Leiden, Leiden University, Sylviusweg 72, 2333 BE Leiden, The Netherlands.
A series of aminocarboxylic acid analogues of aspergillomarasmine A (AMA) and ethylenediamine-N,N'-disuccinic acid (EDDS) were chemoenzymatically synthesized via the addition of various mono- and diamine substrates to fumaric acid catalyzed by the enzyme EDDS lyase. Many of these novel AMA and EDDS analogues demonstrate potent inhibition of the bacterial metallo-β-lactamase NDM-1. Isothermal titration calorimetry assays revealed a strong correlation between the inhibitory potency of the compounds and their ability to bind zinc.
View Article and Find Full Text PDFInorg Chem
October 2019
School of Medical Sciences (Pharmacology) , The University of Sydney, 2006 Sydney , New South Wales , Australia.
An expedited synthesis of -hydroxamic acid aminocarboxylic acid (-HXA) compounds has been developed. These monomeric ligands are relevant to the synthesis of metal-macrocycle complexes using metal-templated synthesis (MTS), and the downstream production of apomacrocycles. Macrocycles can display useful drug properties and be used as ligands for radiometals in medical imaging applications, which supports methodological advances in accessing this class of molecule.
View Article and Find Full Text PDFBiochemistry
July 2018
Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy , University of Groningen, Antonius Deusinglaan 1 , 9713 AV Groningen , The Netherlands.
The natural aminocarboxylic acid product ethylenediamine- N, N'-disuccinic acid [( S, S)-EDDS] is able to form a stable complex with metal ions, making it an attractive biodegradable alternative for the synthetic metal chelator ethylenediaminetetraacetic acid (EDTA), which is currently used on a large scale in numerous applications. Previous studies have demonstrated that biodegradation of ( S, S)-EDDS may be initiated by an EDDS lyase, converting ( S, S)-EDDS via the intermediate N-(2-aminoethyl)aspartic acid (AEAA) into ethylenediamine and two molecules of fumarate. However, current knowledge of this enzyme is limited because of the absence of structural data.
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