Protein films are used as effective lipid, oxygen, and aroma barriers at moderate relative humidity conditions. However, they perform poorly as moisture barriers. The introduction of crosslinks within or between protein chains by enzymatic or chemical modification has been proposed as an alternative means to achieving a stronger polymeric matrix structure, which would result in better functional film properties. In this article, we report the preparation and characterization of sodium caseinate (SC) films crosslinked by glutaraldehyde (GTA) or heat. The crosslinking density increased with GTA content. The thermal stability and tensile modulus and strength increased with GTA content, although films with a low crosslinking density exhibited lower properties than the uncrosslinked sample. Unexpectedly, water vapor permeability and absorption also increased with crosslinking density. The crosslinking of SC was also induced by simple heating. The resulting films showed enhanced thermal, mechanical, and barrier properties compared to the unmodified SC films and even the GTA-crosslinked samples. GTA crosslinking was unable to reduce the high hydrophilicity of the SC films. Thermally induced crosslinking was revealed to be a valid alternative for improving the properties of SC films, without the inherent complications associated with the use of a chemical crosslinking agent.
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