Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain
This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis.
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Language: | English |
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Multidisciplinary Digital Publishing Institute
2020
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Subjects: | Zbasic as “affinity and immobilization tag”, Stabilization of catalase, Instantaneous elimination of hydrogen peroxide inside porous support, |
Online Access: | http://hdl.handle.net/10261/228555 http://dx.doi.org/10.13039/100008054 |
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dig-cial-es-10261-2285552021-02-06T04:40:00Z Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain García-García, Paz Rocha-Martín, Javier Guisán, José Manuel Fernández-Lorente, Gloria Fundación Ramón Areces Zbasic as “affinity and immobilization tag” Stabilization of catalase Instantaneous elimination of hydrogen peroxide inside porous support This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis. 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. This work was financially supported by the Ramon Areces Foundation for the project in the field of Sciences of Life and Matter titled “The detection and elimination of biogenic amines in foods: the design of new biosensors and new amine oxidase catalysts”. The APC was funded by Ramon Areces Foundation. The authors would like to thank the Ramon Areces Foundation for the pre-doctoral grant awarded to Paz García-García. Peer reviewed 2021-02-04T10:24:13Z 2021-02-04T10:24:13Z 2020 artículo http://purl.org/coar/resource_type/c_6501 Catalysts 10(7): 810 (2020) http://hdl.handle.net/10261/228555 10.3390/catal10070810 2073-4344 http://dx.doi.org/10.13039/100008054 en Publisher's version https://doi.org/10.3390/catal10070810 Sí open Multidisciplinary Digital Publishing Institute |
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Zbasic as “affinity and immobilization tag” Stabilization of catalase Instantaneous elimination of hydrogen peroxide inside porous support Zbasic as “affinity and immobilization tag” Stabilization of catalase Instantaneous elimination of hydrogen peroxide inside porous support |
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Zbasic as “affinity and immobilization tag” Stabilization of catalase Instantaneous elimination of hydrogen peroxide inside porous support Zbasic as “affinity and immobilization tag” Stabilization of catalase Instantaneous elimination of hydrogen peroxide inside porous support García-García, Paz Rocha-Martín, Javier Guisán, José Manuel Fernández-Lorente, Gloria Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain |
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This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis. |
author2 |
Fundación Ramón Areces |
author_facet |
Fundación Ramón Areces García-García, Paz Rocha-Martín, Javier Guisán, José Manuel Fernández-Lorente, Gloria |
format |
artículo |
topic_facet |
Zbasic as “affinity and immobilization tag” Stabilization of catalase Instantaneous elimination of hydrogen peroxide inside porous support |
author |
García-García, Paz Rocha-Martín, Javier Guisán, José Manuel Fernández-Lorente, Gloria |
author_sort |
García-García, Paz |
title |
Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain |
title_short |
Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain |
title_full |
Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain |
title_fullStr |
Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain |
title_full_unstemmed |
Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain |
title_sort |
co-immobilization and co-localization of oxidases and catalases: catalase from bordetella pertussis fused with the zbasic domain |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2020 |
url |
http://hdl.handle.net/10261/228555 http://dx.doi.org/10.13039/100008054 |
work_keys_str_mv |
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