Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/90606
Title: Latex dispersions as carriers for glucose oxidase oxygen scavenging systems
Authors: Nestorson, A.
Jansson, A.
Järnstrom, L.
Jönsson, L.
Leufvén, A.
Neoh, K.G. 
Kang, E.T. 
Issue Date: 2008
Citation: Nestorson, A.,Jansson, A.,Järnstrom, L.,Jönsson, L.,Leufvén, A.,Neoh, K.G.,Kang, E.T. (2008). Latex dispersions as carriers for glucose oxidase oxygen scavenging systems. TAPPI Advanced Coating Fundamentals Symposium Proceedings : 456-467. ScholarBank@NUS Repository.
Abstract: In this study the use of enzymes in latex barrier coating in order to create active oxygen absorbing packaging materials was demonstrated. The current paper is a summary of recent research activities. The enzyme glucose oxidase was added to latex dispersions and coating colours. The coating colours were coated on packaging board and used for formation of free films. The enzyme retained its activity also at high drying temperatures if the drying time was not too long. Different drying conditions and paperboards were investigated. The coatings were drawn down on un-coated paperboard as well as PE-laminated paperboard. The coatings also retained its enzyme activity at a high level after long storage times. In this study the enzymes were added to the coating colours by two different methods: (1) by adding non-immobilized (free) enzymes to the coating colour and (2) by using latex particles to which the enzymes have been immobilized onto the latex particle surfaces by covalent bonding. The latter method is assumed to prevent migration of the enzyme. The technique with covalently bonded enzymes resulted in only slightly less enzyme activity than addition of the non-immobilized enzymes did. The results were also compared to immobilization of enzyme on the film surface after complete film formation.
Source Title: TAPPI Advanced Coating Fundamentals Symposium Proceedings
URI: http://scholarbank.nus.edu.sg/handle/10635/90606
ISBN: 1595101748
Appears in Collections:Staff Publications

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