Abstract
Abstract The mechanical, hydrophobic and thermal properties of cast films of vicilin-rich protein isolates from three Phaseolus legumes were investigated and compared to that of soy protein isolate (SPI). The influence of heat curing at 85 °C on the properties of these films was characterized. The films of vicilin-rich protein isolates exhibited much less mechanical strength (TS) and elongation at break (EB) and similar film surface hydrophobicity, as compared with those of the SPI film. The heating remarkably improved the TS of these films, and the extent of the improvement much higher than that of the SPI film, while the EB was only slightly affected. The thermal properties of these protein isolate films were variable, and much distinctly affected by the heating of the films, to a various extent, depending on the type of protein isolates. Protein solubility analyses indicated strengthened hydrogen and hydrophobic bondings of these films by the heating. The results suggest that those vicilin-rich protein isolates have good potential to form cast films with mechanical strength comparable to that of SPI film.
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