Enzymatic Crosslinking Enhance Film Properties of Deamidated Gluten
Covalent bonds were introduced in deamidated gluten films by transglutaminase. The type of cross-links was modulated by adding diamines in the film-forming solution. Biochemical and mechanical properties of the resulting films were investigated. Film properties of deamidated gluten were compared to those of native gluten. Plasticizer content modified considerably the film properties and a ratio of 0.35 was chosen for the following experiments. At this ratio, the addition of increasing diamine concentration in the film solution was shown to have a slight positive plasticizer effect. As shown by SDS PAGE of the film proteins, transglutaminase was efficient in catalysing the formation of polymers in the film solution. The loss of solubility was related to the formation of high molecular weight polymers in the film. In all cases, the action of transglutaminase induced simultaneously an increase in strain and stress of the films. The addition of diamines in the film solution affected more the strain than the stress properties. These diamines, able to react at their two extremities, probably acted as spacers between gluten proteins. The IR study didn’t show any modification of the secondary structure of the proteins in the film. Transglutaminase was efficient in introducing new cross-links in gluten films. This modification enhanced their mechanical properties and modified their solubility properties.
KeywordsFilm Property Edible Film High Molecular Weight Polymer Film Protein Film Solution
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