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首页> 外文期刊>Journal of thermal analysis and calorimetry >Comparative thermostability of whey protein and alginate hydrospheres complexed with divalent cations
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Comparative thermostability of whey protein and alginate hydrospheres complexed with divalent cations

机译:Comparative thermostability of whey protein and alginate hydrospheres complexed with divalent cations

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摘要

Water retention and thermostability of powders and films of whey protein isolate (WPIp, dWPIf), sodium alginate (NaALGp, NaALGf), and their dry hydrospheres were evaluated by thermogravimetric analysis to demonstrate the importance of the gelling cation, for the first time in the case of the protein, and some potential applications. WPIp retained less water (7.1) than ALGp (20.4) due to the greater hydrophilicity of the polysaccharide. The difference was smaller for the films (12.3 and 18.8, respectively) due to the incorporation of water during protein denaturation. Dried ALG beads retained less water than the film and the water content was dependent on the crosslinking cation (CaALGs > ZnALGs > CdALG). Protein films and spheres exhibited water retention very similar to CaALGs. The degradation of ZnALGs (smallest radius cation used and monodentate coordination) began at the lowest temperature (168 degrees C) and exhibited the highest mass loss as compared to CaALGs (171 degrees C) or CdALGs (176 degrees C, both with bidentate coordination). For the protein, Zn2+ also exhibited the lowest degradation peak temperature. Pyrolisis of powders, films and spheres demonstrate that the protein is more stable than the polyssacharide. Therefore, it can act as a better flame retardant agent than alginate. On the other hand, only alginate spheres were suitable for the production of activated carbon (190.0 m(2) g(-1)) and the recovery of metal oxides.
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