Solving the H2O2 by-product problem using a catalase-mimicking nanozyme cascade to enhance glycolic acid oxidase

Jiao, Mengzhao; Li, Zhengjun; Li, Xianglai; Zhang, Zijie; Yuan, Qipeng; Vriesekoop, Frank; Liang, Hao; Liu, Juewen

doi:10.1016/j.cej.2020.124249

Cited by 56 publications

(27 citation statements)

References 47 publications

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“…Indeed, the activity of ALP was fully abolished (Figure C), while the activity of CeO 2 (Figure A) and Ce(IV) (Figure B) remained unchanged. Heat treatment of other nanozymes also showed robust activity compared to protein‐based enzymes …”

Section: Resultsmentioning

confidence: 99%

Self‐limited Phosphatase‐mimicking CeO₂ Nanozymes

Liu

2020

ChemNanoMat

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CeO2 nanoparticles or nanoceria is a very interesting enzyme mimic (nanozyme) with a diverse range of catalytic activities. Most of the previous studies focused on its redox chemistry for mimicking oxidase, peroxidase, and catalase‐like activities, and as a scavenger of reactive oxygen species. Considering CeO2 has both Ce(III) and Ce(IV) species and both interact strongly with inorganic phosphate, nanoceria has also been studied for its phosphatase‐like activity. We herein compared these species along with alkaline phosphatase (ALP). First, CeO2 and Ce(IV) have good activity using p‐nitrophenylphosphate (p‐NPP) as a substrate, while other metal ions failed to show this activity. Since a reaction product is inorganic phosphate and we observed an interesting enzyme kinetic profile, the effect of phosphate was studied, which inhibited both CeO2 and ALP. The inhibition constant was about 5‐fold smaller for CeO2. The inhibition effect of polyphosphates was even stronger. Due to the product inhibition effect, CeO2 is unlikely to be a typical multiple turnover nanozyme, and the system is self‐limited. For the other anions, only F− showed a moderate inhibition effect on the cerium species, while adsorption of DNA did not inhibit the activity. Finally, heat treated ALP lost the activity, but CeO2 and Ce(IV) remained active. This study has deepened our understanding of CeO2 as a phosphatase mimicking nanozyme, which could be useful for biosensing and chemical biology applications.

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Section: Resultsmentioning

confidence: 99%

Self‐limited Phosphatase‐mimicking CeO₂ Nanozymes

Liu

2020

ChemNanoMat

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“…The as‐prepared cascade nanoreactor not only possessed high stability, enhanced catalytic efficiency, and good reusability, but in addition solved the H 2 O 2 by‐product problem in the redox enzyme reactors by using the CAT activity for the decomposition of H 2 O 2 . [ 86 ] In recent research, the group of Su established a cascade system by integrating the natural galactose oxidase (Gal Ox) and Fe‐N‐C SAzyme (Fe‐SAzyme) for a galactose assay. In this cascade system, galactose as the substrate could be oxidized by Gal Ox to produce H 2 O 2 , and the Fe‐SAzyme was used to catalyze H 2 O 2 to achieve TMB oxidation and colorimetric biosensing.…”

Section: Biomimetic Cascade Nanoreactorsmentioning

confidence: 99%

“…Then, in the presence of H 2 O 2 , europium (III)‐tetracycline (Eu‐Tc) was catalyzed by the CAT‐like activity of Fe 3+ /AMP&GyAO nanogel to produce a fluorescent product. [ 86 ] To further improve the performance of fluorescence based biosensing, SAzymes were combined with AChE to generate a cascade reaction system (Figure 9C). Using this fluorescence method, AChE activity could be detected over a liner range from 2 to 70 U L −1 with a LOD of 0.56 U L −1 .…”

Section: Biosensing Applicationsmentioning

confidence: 99%

Enzyme Mimics for Engineered Biomimetic Cascade Nanoreactors: Mechanism, Applications, and Prospects

Zhang

Chen

et al. 2021

Adv Funct Materials

103

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Multiple enzyme-driven biological catalytic cascades occur in living organisms, guiding highly efficient and selective transformations of substrates. Inspired by the merits of these biological catalytic cascade systems, enormous efforts have been devoted to developing novel cascade catalytic systems to mimic biological cascade catalytic reactions over the past few years. Nanozymes, a class of enzyme mimics, are nanomaterials with enzyme-like catalytic activity. The emergence and development of nanozymes has significantly advanced the development of biomimetic cascade nanoreactors. Currently, biomimetic cascade nanoreactors driven by advanced nanozymes have been widely used and exhibit many advantages such as superior cascade catalytic efficiency and high stability, resulting in significant advancements in biosensing and biomedical applications. The latest advances in understanding the cascade catalytic mechanism of nanozyme-engineered biomimetic cascade catalytic nanoreactors and their progressive applications for biosensing and biomedical applications are comprehensively covered here. First, nanozyme and enzyme/nanozyme-engineered biomimetic cascade catalytic nanoreactors are categorized according to their catalytic mechanism and properties. Then, the biosensing and biomedical applications, including cancer therapy, antibacterial activity, antioxidation, and hyperuricemia therapy of the cascade catalytic systems are covered. The conclusion describes the most important challenges and opportunities remaining in this exciting area of research.

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“…In general, this reaction releases hydrogen peroxide, a very undesirable by-product. When designing industrial processes, with very high substrate concentrations, the release of very high concentrations of hydrogen peroxide promotes the dramatic inactivation of the oxidase [4,5]. The decomposition of hydrogen peroxide may be achieved by using an auxiliary catalase able to decompose hydrogen peroxide in water plus oxygen [6].…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization and Co-Localization of Oxidases and Catalases: Catalase from Bordetella Pertussis Fused with the Zbasic Domain

et al. 2020

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Oxidases catalyze selective oxidations by using molecular oxygen as an oxidizing agent. This process promotes the release of hydrogen peroxide, an undesirable byproduct. The instantaneous elimination of hydrogen peroxide can be achieved by co-immobilization and co-localization of the oxidase and an auxiliary catalase inside the porous structure of solid support. In this paper, we proposed that catalase from Bordetella pertussis fused with a small domain (Zbasic) as an excellent auxiliary enzyme. The enzyme had a specific activity of 23 U/mg, and this was almost six-fold higher than the one of the commercially available catalases from bovine liver. The Zbasic domain was fused to the four amino termini of this tetrameric enzyme. Two domains were close in one hemisphere of the enzyme molecule, and the other two were close in the opposite hemisphere. In this way, each hemisphere contained 24 residues with a positive charge that was very useful for the purification of the enzyme via cationic exchange chromatography. In addition to this, each hemisphere contained 10 Lys residues that were very useful for a rapid and intense multipoint covalent attachment on highly activated glyoxyl supports. In fact, 190 mg of the enzyme was immobilized on one gram of glyoxyl-10% agarose gel. The ratio catalase/oxidase able to instantaneously remove more than 93% of the released hydrogen peroxide was around 5–6 mg of catalase per mg of oxidase. Thirty milligrams of amine oxidase and 160 mg of catalase were co-immobilized and co-localized per gram of glyoxyl-agarose 10BCL (10% beads cross-linked) support. This biocatalyst eliminated biogenic amines (putrescine) 80-fold faster than a biocatalyst of the same oxidase co-localized with the commercial catalase from bovine liver.

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Solving the H2O2 by-product problem using a catalase-mimicking nanozyme cascade to enhance glycolic acid oxidase

Cited by 56 publications

References 47 publications

Self‐limited Phosphatase‐mimicking CeO₂ Nanozymes

Self‐limited Phosphatase‐mimicking CeO₂ Nanozymes

Enzyme Mimics for Engineered Biomimetic Cascade Nanoreactors: Mechanism, Applications, and Prospects

Co-Immobilization and Co-Localization of Oxidases and Catalases: Catalase from Bordetella Pertussis Fused with the Zbasic Domain

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Solving the H2O2 by-product problem using a catalase-mimicking nanozyme cascade to enhance glycolic acid oxidase

Cited by 56 publications

References 47 publications

Self‐limited Phosphatase‐mimicking CeO2 Nanozymes

Self‐limited Phosphatase‐mimicking CeO2 Nanozymes

Enzyme Mimics for Engineered Biomimetic Cascade Nanoreactors: Mechanism, Applications, and Prospects

Co-Immobilization and Co-Localization of Oxidases and Catalases: Catalase from Bordetella Pertussis Fused with the Zbasic Domain

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Product

Resources

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Self‐limited Phosphatase‐mimicking CeO₂ Nanozymes

Self‐limited Phosphatase‐mimicking CeO₂ Nanozymes