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Most films used to preserve foodstuffs are made from synthetic plastic materials.However, for environmental reasons, attention has recently turned to biodegradable films. Gelatin has been extensively studied for its film forming capacity and applicability as an outer covering to protect food against drying, light, and oxygen. Moreover, it is 5 one of the first materials proposed as a carrier of bioactive components. Gelatins from alternatives to mammalian species are gaining prominence, especially gelatins from marine fish species. Because of their good film-forming abilities, fish gelatins may be a good alternative to synthetic plastics for making films to preserve foodstuffs. The mechanical and barrier properties of these films depend largely on the physical and 10 chemical characteristics of the gelatin, especially the amino acid composition, which is highly species specific, and the molecular weight distribution, which depends mainly on processing conditions. Different film formulations can be developed to extend the films' physical and chemical properties and to add new functional attributes. This paper reviews the most recent scientific literature dealing with films based on gelatins from 15 different fish species and considers various strategies intended to improve the physical properties of such films by combining fish gelatins with such other biopolymers as soy protein isolate, oils and fatty acids, and certain polysaccharides. The use of plasticizers and cross-linking agents is also discussed. Specific attributes, such as antimicrobial and antioxidant activities, may be also conferred by blending the gelatin 20 with chitosan, lysozyme, essential oils, plant extracts, or vitamin C to produce an active packaging biomaterial.

** This centre has implemented and maintains a Quality Management System which fulfils the requirements of the ISO standard 9001:2000 AbstractSquid gelatin obtained from inner and outer tunics was hydrolyzed with Alcalase to isolate antioxidant peptide sequences. The ACE-inhibitory activity of the isolated peptides was also evaluated. After fractionation by ultrafiltration and size-exclusion chromatography into four fractions, the antioxidant activity of the peptide fractions was determined by radical scavenging ability and ferric reducing power. Fraction FIII showed the highest antioxidant activity, although slight differences could be expected in the antioxidant activity of the different fractions based on the amino acid composition.FIII was subjected to liquid chromatography and tandem mass spectrometry (LC-MS/MS) and two major compounds were identified: the compound with m/z 952.42, which could be mostly comprised by the carbohydrate fucose, and the peptide with m/z 1410.63. Three possible sequences were proposed for this peptide, and the contribution of Leu or Hyp residues to the antioxidant and ACE-inhibitory activities of the resulting sequence was evaluated. The presence of Leu residues in the peptide sequence in *Manuscript Click here to view linked References 2 replacement of Hyp seems to play an important role in the antioxidant and ACEinhibitory activity.

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The structure-function relationship of composite films obtained from soy protein isolate (SPI) and cod gelatin was studied. Films with different ratios of SPI:gelatin (0, 25, 50, 75, 100% w/w) plasticized by a mixture of glycerol and sorbitol, were prepared by casting. Regardless of the soy protein concentration, the thickness and water vapor permeability of the composite films diminished significantly as compared to pure gelatin films. The formulation containing 25% SPI: 75% cod skin gelatin had the maximum force at the breaking point which was 1.8-fold and 2.8-fold of those of 100% gelatin and 100% SPI films, respectively. Moreover, this formulation offered high percent deformation values as the 100% gelatin film and relatively low water vapor permeability as the 100% SPI film. While all the films exhibited high water solubility, a slight reduction of the protein released in water was observed with increasing soy contents. DSC analyses revealed that gelatin was completely denatured in all the films, while the soy proteins maintained most of their native conformation. The FTIR analysis revealed the presence of 25% SPI to produce gelatin conformational changes, self aggregation of gelatin α-chains as well as intermolecular associations through C=O bonds between gelatin and SPI proteins.. Regarding appearance, all the films were translucent, but the yellowish color (b*) increased with increasing proportions of soy proteins.