Transglutaminase-induced crosslinking of gelatin–calcium carbonate composite films. (1st January 2015)

• Record Type: Journal Article
• Authors: Wang, Yuemeng; Liu, Anjun; Ye, Ran; Wang, Wenhang; Li, Xin
• Is Part Of: Food chemistry. Volume 166(2015)
• Page Start: 414
• Page End: 422
• Publication Date: 2015-01-01
• Subjects: Gelatin -- Calcium carbonate -- Transglutaminase -- Composite films; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2014.06.062
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: TGase enhanced the mechanical and barrier properties of gelatin–calcium carbonate composite films. TGase promoted the crosslinking of gelatin–calcium carbonate composite films. Gelatin–calcium carbonate composite films can act as a good edible film in food industries. Abstract: The effects of transglutaminase (TGase) on the rheological profiles and interactions of gelatin–calcium carbonate solutions were studied. In addition, mechanical properties, water vapour permeability and microstructures of gelatin–calcium carbonate films were also investigated and compared. Fluorescence data suggested that the interaction of TGase and gelation-calcium carbonate belonged to a static quenching mechanism, and merely one binding site between TGase and gelatin–calcium carbonate was identified. Moreover, differential scanning calorimetry (DSC), the mechanical properties and the water vapour permeability studies revealed that TGase favoured the strong intramolecular polymerisation of the peptides in gelatin. The microstructures of the surfaces and cross sections in gelatin–calcium carbonate films were shown by scanning electron microscope (SEM) micrographs. The results of the fourier transform infrared spectroscopy (FTIR) indicated that TGase caused conformational changes in the proteins films. Therefore, TGase successfully facilitated the formation of gelatin–calcium carbonate composite films.