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

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.

Saved in:

Bibliographic Details
Main Authors:	García-García, Paz, Rocha-Martín, Javier, Guisán, José Manuel, Fernández-Lorente, Gloria
Other Authors:	Fundación Ramón Areces
Format:	artículo biblioteca
Language:	English
Published:	Multidisciplinary Digital Publishing Institute 2020
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
Tags:	Add Tag No Tags, Be the first to tag this record!

id	dig-cial-es-10261-228555
record_format	koha
spelling	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
institution	CIAL ES
collection	DSpace
country	España
countrycode	ES
component	Bibliográfico
access	En linea
databasecode	dig-cial-es
tag	biblioteca
region	Europa del Sur
libraryname	Biblioteca del CIAL España
language	English
topic	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
spellingShingle	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
description	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	AT garciagarciapaz coimmobilizationandcolocalizationofoxidasesandcatalasescatalasefrombordetellapertussisfusedwiththezbasicdomain AT rochamartinjavier coimmobilizationandcolocalizationofoxidasesandcatalasescatalasefrombordetellapertussisfusedwiththezbasicdomain AT guisanjosemanuel coimmobilizationandcolocalizationofoxidasesandcatalasescatalasefrombordetellapertussisfusedwiththezbasicdomain AT fernandezlorentegloria coimmobilizationandcolocalizationofoxidasesandcatalasescatalasefrombordetellapertussisfusedwiththezbasicdomain
_version_	1777671463135870976

Co-immobilization and co-localization of oxidases and catalases: Catalase from Bordetella pertussis fused with the Zbasic domain

Similar Items

Resource Map