Change search
ReferencesLink to record
Permanent link

Direct link
Co-immobilization of oxalate oxidase and catalase in films for scavenging of oxygen or oxalic acid
Kemiska institutionen, Department of Chemistry, Umeå Universitet.
Karlstad University, Faculty of Technology and Science, Department of Chemical Engineering.
Karlstad University, Faculty of Technology and Science, Department of Chemical Engineering. (Paper Surface Centre)ORCID iD: 0000-0002-1256-1708
Kemiska institutionen, Department of Chemistry, Umeå Universitet.
2013 (English)In: Biochemical engineering journal, ISSN 1369-703X, E-ISSN 1873-295X, Vol. 72, 96-101 p.Article in journal (Refereed) Published
Abstract [en]

Oxalate oxidase has potential to act as an oxygen scavenger in active packaging to increase the shelf-life of food and beverages, while simultaneously producing the protective packaging gas carbon dioxide. This study shows that oxalate oxidase from barley can be immobilized with retained catalytic activity through entrapment in a latex polymer matrix. Conditions for formation of film containing oxalate oxidase have been evaluated as well as effects of storage and latex on enzyme activity, migration of enzyme in films, and the ability of the latex films to resist higher temperatures. Drying of enzyme-containing latex films at 75 °C prior to conditioning at 30 °C resulted in higher activity than drying solely at 30 °C, or drying at 95 °C or 105 °C followed by conditioning at 30 °C. Storage of films in air at 4 °C for 14 days did not negatively affect the enzymatic activity. Inclusion of catalase in films with oxalate oxidase effectively prevented release of hydrogen peroxide. The results suggest that the immobilized enzyme can successfully be used both as an oxygen scavenger and as an oxalic-acid scavenger.

Place, publisher, year, edition, pages
2013. Vol. 72, 96-101 p.
Keyword [en]
Oxalate oxidase, active packaging, oxygen scavenger, oxalic acid, latex, entrapment
National Category
Industrial Biotechnology Chemical Engineering
URN: urn:nbn:se:kau:diva-26574DOI: 10.1016/j.bej.2013.01.006ISI: 000319373200014OAI: diva2:609561
Available from: 2013-03-06 Created: 2013-03-06 Last updated: 2015-12-15Bibliographically approved
In thesis
1. Oxygen-reducing enzymes in coatings and films for active packaging
Open this publication in new window or tab >>Oxygen-reducing enzymes in coatings and films for active packaging
2013 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Oxygen scavengers are used in active packages to protect the food against deteriorative oxidation processes. The aim of this work was to investigate the possibilities to produce oxygen-scavenging packaging materials based on oxygen-reducing enzymes. The enzymes were incorporated into a dispersion coating formulation applied onto a food-packaging board using conventional laboratory coating techniques.

Various enzymes were used: a glucose oxidase, an oxalate oxidase and three laccases originating from different organisms. All of the enzymes were successfully incorporated into a coating layer and could be reactivated after drying. For at least two of the enzymes, re-activation was possible not only by using liquid water but also by using water vapour. Re-activation of the glucose oxidase and a laccase required relative humidities of greater than 75% and greater than 92%, respectively.

Catalytic reduction of oxygen gas by glucose oxidase was promoted by creating an open structure through addition of clay to the coating at a level above the critical pigment volume concentration. Migration of the enzyme and the substrate was reduced by adding an extrusion-coated liner of polypropylene on top of the coating.

For the laccase-catalysed reduction of oxygen it was possible to use lignin derivatives as substrates for the enzymatic reaction. The laccase-catalysed reaction created a polymeric network by cross-linking of lignin-based entities, which resulted in increased stiffness and increased water-resistance of biopolymer films. The laccases were also investigated with regard to their potential to function as oxygen scavengers at low temperatures. At 7°C all three laccases retained more than 20% of the activity they had at room temperature (25°C), which suggests that the system is also useful for packaging of refrigerated food.

Place, publisher, year, edition, pages
Karlstad: Karlstads universitet, 2013. 91 p.
Karlstad University Studies, ISSN 1403-8099 ; 2013:38
Active packaging, food packaging, oxygen scavengers, oxygen-reducing enzymes, dispersion coating, biopolymers
National Category
Chemical Engineering
Research subject
Chemical Engineering
urn:nbn:se:kau:diva-28749 (URN)978-91-7063-516-8 (ISBN)
Public defence
2013-10-18, 9C204, Rejmersalen, Karlstad, 10:15 (English)
Available from: 2013-09-27 Created: 2013-08-27 Last updated: 2014-10-27Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Johansson, KristinJärnström, Lars
By organisation
Department of Chemical Engineering
In the same journal
Biochemical engineering journal
Industrial BiotechnologyChemical Engineering

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 59 hits
ReferencesLink to record
Permanent link

Direct link