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Energy-saving and product-oriented hydrogen peroxide electrosynthesis enabled by electrochemistry pairing and product engineering.

ABSTRACT: Hydrogen peroxide (H₂O₂) electrosynthesis through oxygen reduction reaction (ORR) is drawing worldwide attention, whereas suffering seriously from the sluggish oxygen evolution reaction (OER) and the difficult extraction of thermodynamically unstable H₂O₂. Herein, we present an electrosynthesis protocol involving coupling ORR-to-H₂O₂ with waste polyethylene terephthalate (PET) upcycling and the first H₂O₂ conversion strategy. Ni-Mn bimetal- and onion carbon-based catalysts are designed to catalyze ORR-to-H₂O₂ and ethylene glycol electrooxidation with the Faradaic efficiency of 97.5% (H₂O₂) and 93.0% (formate). This electrolysis system runs successfully at only 0.927 V to achieve an industrial-scale current density of 400 mA cm^-2, surpassing all reported H₂O₂ electrosynthesis systems. H₂O₂ product is upgraded through two downstream routes of converting H₂O₂ into sodium perborate and dibenzoyl peroxide. Techno-economic evolution highlights the high gross profit of the ORR || PET upcycling protocol over HER || PET upcycling and ORR || OER. This work provides an energy-saving methodology for the electrosynthesis of H₂O₂ and other chemicals.

SUBMITTER: Qi J

PROVIDER: S-EPMC10560254 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

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Energy-saving and product-oriented hydrogen peroxide electrosynthesis enabled by electrochemistry pairing and product engineering.

Qi Jun J Du Yadong Y Yang Qi Q Jiang Na N Li Jiachun J Ma Yi Y Ma Yangjun Y Zhao Xin X Qiu Jieshan J

Nature communications 20231007 1

Hydrogen peroxide (H2O2) electrosynthesis through oxygen reduction reaction (ORR) is drawing worldwide attention, whereas suffering seriously from the sluggish oxygen evolution reaction (OER) and the difficult extraction of thermodynamically unstable H2O2. Herein, we present an electrosynthesis protocol involving coupling ORR-to-H2O2 with waste polyethylene terephthalate (PET) upcycling and the first H2O2 con ...[more]

PMID: 37805528

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Project description:BackgroundThe ability of fungal cellobiose dehydrogenase (CDH) to generate H2O2 in-situ is highly interesting for biotechnological applications like cotton bleaching, laundry detergents or antimicrobial functionalization of medical devices. CDH's ability to directly use polysaccharide derived mono- and oligosaccharides as substrates is a considerable advantage compared to other oxidases such as glucose oxidase which are limited to monosaccharides. However CDH's low activity with oxygen as electron acceptor hampers its industrial use for H2O2 production. A CDH variant with increased oxygen reactivity is therefore of high importance for biotechnological application. Uniform expression levels and an easy to use screening assay is a necessity to facilitate screening for CDH variants with increased oxygen turnover.ResultsA uniform production and secretion of active Myriococcum thermophilum CDH was obtained by using Saccharomyces cerevisiae as expression host. It was found that the native secretory leader sequence of the cdh gene gives a 3 times higher expression than the prepro leader of the yeast α-mating factor. The homogeneity of the expression in 96-well deep-well plates was good (variation coefficient <15%). A high-throughput screening assay was developed to explore saturation mutagenesis libraries of cdh for improved H2O2 production. A 4.5-fold increase for variant N700S over the parent enzyme was found. For production, N700S was expressed in P. pastoris and purified to homogeneity. Characterization revealed that not only the kcat for oxygen turnover was increased in N700S (4.5-fold), but also substrate turnover. A 3-fold increase of the kcat for cellobiose with alternative electron acceptors indicates that mutation N700S influences the oxidative- and reductive FAD half-reaction.ConclusionsSite-directed mutagenesis and directed evolution of CDH is simplified by the use of S. cerevisiae instead of the high-yield-host P. pastoris due to easier handling and higher transformation efficiencies with autonomous plasmids. Twelve clones which exhibited an increased H2O2 production in the subsequent screening were all found to carry the same amino acid exchange in the cdh gene (N700S). The sensitive location of the five targeted amino acid positions in the active site of CDH explains the high rate of variants with decreased or entirely abolished activity. The discovery of only one beneficial exchange indicates that a dehydrogenase's oxygen turnover is a complex phenomenon and the increase therefore not an easy target for protein engineering.

Dataset Information

Energy-saving and product-oriented hydrogen peroxide electrosynthesis enabled by electrochemistry pairing and product engineering.

Publications

Energy-saving and product-oriented hydrogen peroxide electrosynthesis enabled by electrochemistry pairing and product engineering.

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