Nowadays, the specificity of enzymatic processes makes them more and more important every year, and their usage on an industrial scale seems to be necessary. Enzymatic cofactors, however, play a crucial part in the prospective applications of enzymes, because they are indispensable for conducting highly effective biocatalytic activities. Due to the relatively high cost of these compounds and their consumption during the processes carried out, it has become crucial to develop systems for cofactor regeneration. Therefore, in this review, an attempt was made to summarize current knowledge on enzymatic regeneration methods, which are characterized by high specificity, non-toxicity and reported to be highly efficient. The regeneration of cofactors, such as nicotinamide dinucleotides, coenzyme A, adenosine 5'-triphosphate and flavin nucleotides, which are necessary for the proper functioning of a large number of enzymes, is discussed, as well as potential directions for further development of these systems are highlighted. This review discusses a range of highly effective cofactor regeneration systems along with the productive synthesis of many useful chemicals, including the simultaneous renewal of several cofactors at the same time. Additionally, the impact of the enzyme immobilization process on improving the stability and the potential for multiple uses of the developed cofactor regeneration systems was also presented. Moreover, an attempt was made to emphasize the importance of the presented research, as well as the identification of research gaps, which mainly result from the lack of available literature on this topic.
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http://dx.doi.org/10.1016/j.scitotenv.2023.161630 | DOI Listing |
Appl Biochem Biotechnol
January 2025
Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Cyanobacteria are advantageous hosts for industrial applications toward achieving sustainable society due to their unique and superior properties such as atmospheric CO fixation via photosynthesis. However, cyanobacterial productivities tend to be weak compared to heterotrophic microbes. To enhance them, it is necessary to understand the fundamental metabolic mechanisms unique to cyanobacteria.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Key Laboratory of Organosilicon Chemistry and Materials Technology, Ministry of Education; College of Materials Chemistry and Chemical Engineering, Hangzhou Normal University, Hangzhou, Zhejiang 311121, China. Electronic address:
Keto reductases are crucial NAD(P)H-dependent enzymes used for the enantioselective synthesis of alcohols from prochiral ketones. Typically, the NADPH cofactor is regenerated through a second enzyme and/or substrate. However, photocatalytic cofactor regeneration using water as a sacrificial electron and hydrogen donor presents a promising alternative, albeit a challenging one.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
School of Biotechnology, Jiangnan University, Wuxi 214122, China. Electronic address:
7β-Hydroxysteroid dehydrogenase (7β-HSDH) catalyzes the reversible reaction between 7-ketolithocholic acid (7K-LCA) and ursodeoxycholic acid (UDCA). However, its much lower forward reaction activity led to the unsatisfactory UDCA production. Here, by autodocking 7K-LCA and UDCA into the structure of Hyphomicrobium sp.
View Article and Find Full Text PDFAdv Sci (Weinh)
December 2024
State Key Laboratory of Fine Chemicals, Frontier Science Center for Smart Materials, Dalian University of Technology, Dalian, Liaoning, 116024, China.
Cofactors such as nicotinamide adenine dinucleotide (NADH) and its phosphorylated form (NADPH) play a crucial role in natural enzyme-catalyzed reactions for the synthesis of chemicals. However, the stoichiometric supply of NADH for artificial synthetic processes is uneconomical. Here, inspired by the process of cofactor NADPH regeneration in photosystem I (PSI), catalyst-modified photocathodes are constructed on the surface of polythiophene-based semiconductors (PTTH) via self-assembly for photoelectrochemical catalytic NADH regeneration.
View Article and Find Full Text PDFPhotochem Photobiol Sci
December 2024
Biophysical Chemistry and Diagnostics, Department of Chemistry, Bielefeld University, Universitätsstraße 25, 33615, Bielefeld, Germany.
Flavin-dependent halogenases (FDHs) are promising candidates for the sustainable production of halogenated organic molecules by biocatalysis. FDHs require only oxygen, halide and a fully reduced flavin adenine dinucleotide (FADH) cofactor to generate the reactive HOX that diffuses 10 Å to the substrate binding pocket and enables regioselective oxidative halogenation. A key challenge for the application of FDHs is the regeneration of the FADH.
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