A bovine-hide gelatin and a tuna-skin gelatin, both characterized on the basis of their amino acid composition and molecular weight distribution, were used to prepare edible films by casting with glycerol and sorbitol added as plasticizers. The molecular weight distribution of the tuna-skin gelatin exhibited appreciably higher quantities of beta-components (covalently linked alpha-chain dimers), whereas bovine-hide gelatin showed a certain degradation of alpha(1)-chains being indicative of a greater proteolysis. Intrinsic differences in the gelatin attributes affected in diverse manner some of the physical properties of the films. Thus, water vapour permeability was higher in the bovine-hide gelatin film. whereas deformability was considerably higher (10 times higher) in the tuna-skin gelatin film. In contrast, breaking force and water solubility were basically unaffected by gelatin origin. Analysis of the thermal properties revealed both films to be wholly amorphous with similar glass transition temperature values thanks to the plasticizing effects of the glycerol and sorbitol and the low moisture contents. (C) 2008 Elsevier Ltd. All rights reserved.