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Oxygen-reducing enzymes in coatings and films for active packaging
Karlstad University, Faculty of Health, Science and Technology (starting 2013), Department of Engineering and Chemical Sciences.
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.
Series
Karlstad University Studies, ISSN 1403-8099 ; 2013:38
Keyword [en]
Active packaging, food packaging, oxygen scavengers, oxygen-reducing enzymes, dispersion coating, biopolymers
National Category
Chemical Engineering
Research subject
Chemical Engineering
Identifiers
URN: urn:nbn:se:kau:diva-28749ISBN: 978-91-7063-516-8 (print)OAI: oai:DiVA.org:kau-28749DiVA: diva2:643381
Public defence
2013-10-18, 9C204, Rejmersalen, Karlstad, 10:15 (English)
Opponent
Supervisors
Available from: 2013-09-27 Created: 2013-08-27 Last updated: 2014-10-27Bibliographically approved
List of papers
1. Oxygen scavenging enzymes in coatings: Effect of coating procedures on enzyme activity
Open this publication in new window or tab >>Oxygen scavenging enzymes in coatings: Effect of coating procedures on enzyme activity
2011 (English)In: Nordic Pulp & Paper Research Journal, ISSN 0283-2631, E-ISSN 2000-0669, Vol. 26, no 2, 197-204 p.Article in journal (Refereed) Published
Abstract [en]

The oxygen content in food packaging may be reduced by attaching oxygen scavengers to the packaging material. The critical parameters that determine the oxygen-scavenging ability of an enzyme-based coating i.e. pH, heat and coating color formulation were evaluated. Glucose oxidase, catalase and glucose were added to latex dispersions in the preparation of the coating colors. The enzymes were entrapped in the coating layers after coating and drying. The clay concentration and drying conditions were varied and the enzymatic activity of the coated layer was evaluated. The need for a pH-buffered system was also studied and the results indicated that, when using a carboxylated latex of a standard coating grade, a buffered system was not needed. A rapid drying at a high temperature was preferred over a slow drying at a low temperature in order to prevent pre-oxidation of the substrate in the wet coating color. The scavenging capacity of the coating was dependent on the amount of substrate for the enzyme reaction left after complete drying. The concentration of clay in the coating formulation was shown to have a marked impact on the oxygen-scavenging ability of the coated layer. The enzyme activity was increased by the addition of clay up to a pigment volume concentration (PVC) of ca. 10%. At higher concentrations of clay, the enzyme activity decreased until the critical pigment volume concentration (CPVC) was reached, probably due to the prevention of diffusion of oxygen and consumption of glucose in the coating process before the layer was completely dried. Further additions of clay above the CPVC resulted in an increased enzyme activity, probably due to the creation of a porous structure.

Place, publisher, year, edition, pages
Stockholm: Mittuniversitetet, 2011
Keyword
Enzyme activity, Oxidation, Oxygen, Packaging materials, Scavenging
National Category
Chemical Engineering Chemical Sciences Industrial Biotechnology
Identifiers
urn:nbn:se:kau:diva-15069 (URN)000291334400004 ()
Available from: 2012-10-26 Created: 2012-10-02 Last updated: 2017-12-07Bibliographically approved
2. Evaluation of the potential of fungal and plant laccases for active-packaging applications
Open this publication in new window or tab >>Evaluation of the potential of fungal and plant laccases for active-packaging applications
2011 (English)In: Journal of Agricultural and Food Chemistry, ISSN 0021-8561, E-ISSN 1520-5118, Vol. 59, no 10, 5390-5395 p.Article in journal (Refereed) Published
Abstract [en]

Laccases from Trametes versicolor (TvL), Myceliophthora thermophila (MtL), and Rhus vernicifera (RvL) were investigated with regard to their potential utilization as oxygen scavengers in active packages containing food susceptible to oxidation reactions. The substrate selectivity of the laccases was investigated with a set of 17 reducing substrates, mainly phenolic compounds. The temperature dependence of reactions performed at low temperatures (4-31 C) was studied. Furthermore, the laccases were subjected to immobilization in a latex/clay matrix and drying procedures performed at temperatures up to 105 C. The results show that it is possible to immobilize the laccases with retained activity after dispersion coating, drying at 75-105 C, and subsequent storage of the enzyme-containing films at 4 C. TvL and, to some extent, MtL were promiscuous with regard to their reducing substrate, in the sense that the difference in activity with the 17 substrates tested was relatively small. RvL, on the other hand, showed high selectivity, primarily toward substrates resembling its natural substrate urushiol. When tested at 7 C, all three laccases retained 20% of the activity they had at 25 C, which suggests that it would be possible to utilize the laccases also in refrigerated food packages. Coating and drying resulted in a remaining enzymatic activity ranging from 18 to 53%, depending on the drying conditions used. The results indicate that laccases are useful for active-packaging applications and that the selectivity for reducing substrates is an important characteristic of laccases from different sources. 2011 American Chemical Society.

Place, publisher, year, edition, pages
WASHINGTON: American Chemical Society (ACS), 2011
Keyword
Substrates, Chip scale packages, Coatings, Drying, Packaging, Phenols, Scavenging
National Category
Natural Sciences
Research subject
Chemical Engineering
Identifiers
urn:nbn:se:kau:diva-15070 (URN)10.1021/jf103811g (DOI)000290691300029 ()21524087 (PubMedID)
Note

Trametes versicolor

Available from: 2012-10-26 Created: 2012-10-02 Last updated: 2017-12-07Bibliographically approved
3. Co-immobilization of oxalate oxidase and catalase in films for scavenging of oxygen or oxalic acid
Open this publication in new window or tab >>Co-immobilization of oxalate oxidase and catalase in films for scavenging of oxygen or oxalic acid
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.

Keyword
Oxalate oxidase, active packaging, oxygen scavenger, oxalic acid, latex, entrapment
National Category
Industrial Biotechnology Chemical Engineering
Identifiers
urn:nbn:se:kau:diva-26574 (URN)10.1016/j.bej.2013.01.006 (DOI)000319373200014 ()
Available from: 2013-03-06 Created: 2013-03-06 Last updated: 2017-12-06Bibliographically approved
4. The effects of coating structure and water-holding capacity on the oxygen-scavenging ability of enzymes embedded in the coating layer
Open this publication in new window or tab >>The effects of coating structure and water-holding capacity on the oxygen-scavenging ability of enzymes embedded in the coating layer
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2013 (English)In: TAPPI Journal, ISSN 0734-1415, Vol. 12, no 6, 43-52 p.Article in journal (Refereed) Published
Abstract [en]

Enzymes catalyzing oxygen scavenging were embedded in latex-based coatings with and without barrier kaolin clay to produce material for active packages. The clay was used to create a porous structure, and the closed-structure matrix consisted of a biopolymer comprising either starch or gelatin to increase the water uptake of the coating. The effects of the porous open structure and of the water uptake of the coated layer on the oxygen-scavenging ability of the embedded enzymes were examined at both 75% and 100% relative humidity. The results showed that the porous clay structure led to higher oxygen-scavenging capacity than that of a closed structure at both test conditions by enabling a high diffusion rate for oxygen and glucose to the active sites of the enzymes. The addition of a water-holding biopolymer did not always significantly affect the oxygen-scavenging capacity. However for a less-porous layer at 100% relative humidity, an increase in the amount of biopolymer resulted in an increase in oxygen-scavenging capacity. The results were treated statistically using multiple-factor analysis where the most important factor for the oxygen-scavenging ability was found to be the addition of clay. The coatings were also characterized with respect to water vapor uptake, overall migration, porosity, and scanning electron microscopy images.

Place, publisher, year, edition, pages
TAPPI Press, 2013
Keyword
Active packaging, oxygen scavenging, enzymes, coating
National Category
Chemical Engineering Industrial Biotechnology
Research subject
Chemical Engineering
Identifiers
urn:nbn:se:kau:diva-28458 (URN)000321046600005 ()
Available from: 2013-07-08 Created: 2013-07-08 Last updated: 2017-12-06Bibliographically approved
5. Extruded polymer films for optimal enzyme-catalyzed oxygen scavenging
Open this publication in new window or tab >>Extruded polymer films for optimal enzyme-catalyzed oxygen scavenging
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2014 (English)In: Chemical Engineering Science, ISSN 0009-2509, E-ISSN 1873-4405, Vol. 108, 1-8 p.Article in journal (Refereed) Published
Abstract [en]

The use of enzymes as oxygen scavengers has a great potential in the food packaging industry. Enzymes can be incorporated into a coating layer that can be applied directly onto the packaging material. For the system to be fully functional, there is however a need for the packaging to have some barrier properties, to be sealable through heat, and to ensure low or no migration of the active coating to the food. Various combinations of the polypropylene (PP), poly(lactic acid) (PLA) and low density polyethylene (LDPE) were extruded onto board coated with the oxygen-scavenging enzyme. Properties such as oxygen-transmission rate, water-vapor transmission rate, heat-sealability, migration and oxygen scavenging capacity were evaluated. All combinations of extruded material resulted in a packaging material able to scavenge the oxygen at both 84% and 100% relative humidity. The greatest decrease in oxygen concentration of the head space of air-tight chambers was achieved with the material extruded with PLA on at least one side. It was found that the extruded plastic is necessary in order to meet the EU directives on migration from food packaging materials of not more than a total of 10 mg/dm2 material. All plastics were heat sealable against themselves but not against any of the other plastics and only LDPE adhered strongly to the enzyme-containing coating

Place, publisher, year, edition, pages
Amsterdam: Elsevier, 2014
Keyword
Oxygen scavenging, glucose oxidase, water vapor, migration, extrusion coating
National Category
Chemical Engineering Industrial Biotechnology
Research subject
Chemical Engineering
Identifiers
urn:nbn:se:kau:diva-28460 (URN)10.1016/j.ces.2013.12.035 (DOI)000332392100001 ()
Available from: 2013-07-08 Created: 2013-07-08 Last updated: 2017-12-06Bibliographically approved
6. Oxygen-scavenging coatings and films based on lignosulfonates and laccase
Open this publication in new window or tab >>Oxygen-scavenging coatings and films based on lignosulfonates and laccase
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2012 (English)In: Journal of Biotechnology, ISSN 0168-1656, Vol. 161, no 1, 14-18 p.Article in journal (Refereed) Published
Abstract [en]

Laccase and lignosulfonates were included in coating colors and embedded in latex-based or starch-based films and coatings on foil or board. After 6 days at 23C and 100% relative humidity, the oxygen content in airtight chambers decreased from 1.0% (synthetic gas consisting of 99% N2 and 1% O2) to 0.3% in the presence of board coated with lignosulfonate and laccase, while the oxygen content remained unchanged in control experiments without enzyme. The water stability of lignosulfonate-containing latex-based coatings and starch-based films was improved after laccase-catalyzed oxidation of lignosulfonates, which indicates polymerization to products with lower solubility in water. Furthermore, the E' modulus of starch-based films increased with 30%, which indicates laccase-catalyzed polymerization of lignosulfonates resulting in increased stiffness of the film. The results suggest that laccases and lignosulfonates can be used as an oxygen-scavenging system in active packaging and that enzyme-catalyzed polymerization of lignosulfonates contributes to improved water stability and mechanical properties. 2012 Elsevier B.V.

Place, publisher, year, edition, pages
Amsterdam: Elsevier, 2012
Keyword
Coatings, Catalysis, Enzymes, Latexes, Mechanical properties, Polymerization, Scavenging, Starch
National Category
Chemical Engineering Chemical Sciences
Research subject
Chemistry
Identifiers
urn:nbn:se:kau:diva-15068 (URN)10.1016/j.jbiotec.2012.06.004 (DOI)000306662800002 ()22721759 (PubMedID)
Note

Water stability

Available from: 2012-10-26 Created: 2012-10-02 Last updated: 2015-10-19Bibliographically approved
7. Comparison of lignin derivatives as substrates for laccase-catalyzed scavenging of oxygen in coatings and films
Open this publication in new window or tab >>Comparison of lignin derivatives as substrates for laccase-catalyzed scavenging of oxygen in coatings and films
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(English)Manuscript (preprint) (Other academic)
Abstract [en]

Background: Lignin derivatives are phenylpropanoid biopolymers derived from pulping and biorefinery processes. The possibility to utilize lignin derivatives from different types of processes in advanced enzyme-catalyzed oxygen-scavenging systems intended for active packaging was explored. Laccase-catalyzed oxidation of alkali lignin (LA), hydrolytic lignin (LH), organosolv lignin (LO), and lignosulfonates (LS) was compared using oxygen-scavenging coatings and films in liquid and gas phase systems.

Results: When coatings containing lignin derivatives and laccase were immersed in a buffered aqueous solution, the oxygen-scavenging capability increased in the order LO < LH < LA < LS. Experiments with coatings containing laccase and LO, LH or LA incubated in oxygen-containing gas in air-tight chambers and at a relative humidity (RH) of 100% showed that paperboard coated with LO and laccase reduced the oxygen content from 1.0% to 0.4% during a four-day period, which was far better than the results obtained with LA or LH. LO-containing coatings incubated at 92% RH also displayed activity, with a decrease in oxygen from 1.0% to 0.7% during a four-day period. The oxygen scavenging was not related to the content of free phenolic hydroxyl groups, which increased in the order LO < LS < LH < LA. LO and LS were selected for further studies and films containing starch, clay, glycerol, laccase and LO or LS were characterized using gel permeation chromatograpy, dynamic mechanical analysis, and wet stability.

Conclusions: The investigation shows that different lignin derivatives exhibit widely different properties as a part of active coatings and films. Results indicate that LS and LO were most suitable for the application studied and differences between them were attributed to a higher degree of laccase-catalyzed cross-linking of LS than of LO. Inclusion in active-packaging systems offers a new way to utilize some types of lignin derivatives from biorefining processes.

Keyword
Lignin derivatives, Laccase, Coating, Film, Oxygen scavenger
National Category
Chemical Sciences Chemical Engineering Industrial Biotechnology
Identifiers
urn:nbn:se:kau:diva-28461 (URN)
Available from: 2013-07-08 Created: 2013-07-08 Last updated: 2017-12-06Bibliographically approved

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