Co-localization of oxidase and catalase inside a porous support to improve the elimination of hydrogen peroxide: Oxidation of biogenic amines by amino oxidase from Pisum sativum

García-García, Paz; Rocha-Martín, Javier; Fernández‐Lorente, Gloria

doi:10.1016/j.enzmictec.2018.05.002

Cited by 26 publications

(17 citation statements)

References 33 publications

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“…In this way, each molecule of the main enzyme will be surrounded by several molecules of the auxiliary enzyme, and the nascent hydrogen peroxide will be instantaneously eliminated. The use of very active auxiliary catalases and a suitable ratio of catalase/oxidase are the key points for the accurate preparation of these interesting biocatalysts [11]. These biocatalysts should contain a high concentration of catalase for the instantaneous elimination of hydrogen peroxide but also a high concentration of the main oxidase in order to catalyze the very rapid oxidation of the main substrate.…”

Section: Introductionmentioning

confidence: 99%

“…As a protocol for the co-localization of two enzymes inside porous support, we proposed a two-step process: (i) firstly, a relatively slow immobilization of the main enzyme (oxidase) in order to achieve its homogeneous distribution across the support surface [11] and (ii) secondly, with the support still activated, a very fast full loading of the support surface with the auxiliary enzyme (catalase). In this way, each molecule of the main enzyme (oxidase) would be surrounded by several molecules of auxiliary enzymes, and the molecules of both enzymes would be very close to one another.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Introductionmentioning

confidence: 99%

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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“…Co-immobilization could facilitate in situ removal of by-products, and is essential for reactions that require cofactor regeneration [14,15]. Co-immobilization of the main and regeneration enzymes can also facilitate the mobility of the co-factor between two enzymes.…”

Section: Introductionmentioning

confidence: 99%

Co-immobilized Alcohol Dehydrogenase and Glucose Dehydrogenase with Resin Extraction for Continuous Production of Chiral Diaryl Alcohol

Zhou

Zhang

et al. 2021

Appl Biochem Biotechnol

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Ni 2+ -functionalized porous ceramic/agarose composite beads (Ni-NTA Cerose) can be used as carrier materials to immobilize enzymes harboring a metal affinity tag. Here, a 6×His-tag fusion alcohol dehydrogenase Mu-S5 and glucose dehydrogenase from Bacillus megaterium (BmGDH) were co-immobilized on Ni-NTA Cerose to construct a packed bed reactor (PBR) for the continuous synthesis of the chiral intermediate (S)-(4-chlorophenyl)-(pyridin-2-yl) methanol [(S)-CPMA]. NADPH recycling and in situ product adsorption was achieved simultaneously by assembling a D101 macroporous resin column after the PBR. Using an optimum enzyme activity ration of 2:1 (Mu-S5: BmGDH) and hydroxypropyl-β-cyclodextrin as co-solvent, a space-time yield of 1,560 g/(L•d) could be achieved in the first three days at a flow rate of 5 mL/min and substrate concentration of 10 mM. With simplified selective adsorption and extraction procedures, (S)-CPMA was obtained in 84% isolated yield.

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“…The spatial distance between the active sites of the different enzymes immobilized on the same carrier is shorter than in separately immobilized enzymes, which facilitates the efficient shuttling of the reaction intermediates in the cascade reaction, and thus brings about an improvement in reaction velocity [31,36]. These intermediates either affect the yield of the final product, or inactivate the activity of all the enzymes involved [37,38,39,40,41]. For instance, as co-immobilized tri-enzymes are comprised of glycerol dehydrogenase, NADH oxidase and catalase were employed to produce 1,3-dihydroxyacetone.…”

Section: Introductionmentioning

confidence: 99%

“…Inspired by previous published work, to address problems in the oxidation of HMF, in this work enzyme co-immobilization technology was adopted because of the following reasons: (I) the enhanced rigidity of enzyme conformation via immobilization would lead to improved tolerance of the three enzymes towards the inactivation effect of HMF at a high concentration due to the multiple attachments between the enzymes and the carrier [29,43,44]; (II) the proximity effect offered by co-immobilized enzymes should be of benefit by weakening the toxic effect of hydrogen peroxide on the three enzymes during the oxidation reaction, by rapidly eliminating the hydrogen peroxide produced in the presence of a high concentration of HMF [40,41,42]; (III) the co-immobilization of enzymes would enable the reuse of the three enzymes, to reduce the cost in DFF production.…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Shi

et al. 2019

Molecules

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Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu3(PO4)2 nanoflowers in this study. The resulting co-immobilized tri-enzymes possessed better tolerance towards the oxidative damage caused by hydroxymethylfurfural at high concentrations, as compared to free tri-enzymes. Moreover, the 2,5-diformylfuran yield of co-immobilized tri-enzymes (95.7 ± 2.7%) was 1.06 times higher than that of separately immobilized enzymes (90.4 ± 1.9%). This result could be attributed to the boosted protective effect provided by catalase to the activity of galactose oxidase, owing to the physical proximity between them on the same support. After 30 recycles, co-immobilized tri-enzymes still achieves 86% of the initial yield. Moreover, co-immobilized tri-enzymes show enhanced thermal stability compared with free tri-enzymes. This work paves the way for the production of 2,5-diformylfuran from hydroxymethylfurfural via co-immobilized tri-enzymes.

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Co-localization of oxidase and catalase inside a porous support to improve the elimination of hydrogen peroxide: Oxidation of biogenic amines by amino oxidase from Pisum sativum

Cited by 26 publications

References 33 publications

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

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

Co-immobilized Alcohol Dehydrogenase and Glucose Dehydrogenase with Resin Extraction for Continuous Production of Chiral Diaryl Alcohol

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

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