Journal
FOOD HYDROCOLLOIDS
Volume 45, Issue -, Pages 83-92Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2014.10.008
Keywords
Chicken skin gelatin; Whey protein isolate; Interactions; Rheology; Differential scanning calorimetry; Microstructure
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Physical, thermal and microstructural properties of whey protein isolate (WPI) and unutilized chicken skin gelatin mixtures were investigated for the first time. Small deformation rheology indicated that combinations of gelatin (3, 5 and 10%) and 10% whey protein (WPI) in distilled water produced high elastic modulus (G') values of 1860, 23,914 and 20,145 Pa, respectively, compared with 120 Pa for 10% WPI alone, due to synergistic interaction. Frequency sweeps showed increased strength of networks in gels containing higher gelatin concentrations in WPI/gelatin mixtures. Gelatin gels were more stable and stronger than 10% (w/w) whey protein gels and did not exhibit frequency dependence for G' and G''. Large deformation gel strength values of all samples increased significantly (p < 0.05) with increasing gelatin concentration and were greater at each concentration compared to gelatin alone. Differential scanning calorimetry transition temperature (T-m) and enthalpy change (H) of gelatin and whey protein mixed in the ratios 3:10, 5:10 and 10:10 (w/w) confirmed gelatin reversibility on heating to 90 degrees C and cooling to 10 degrees C and irreversible denaturation of WPI on heating. The addition of 3, 5 or 10% gelatin to whey protein increased whey protein Tm and decreased gelatin Tm. However, the presence of 10% (w/w) WPI significantly increased the Delta H values to 0.62, 1.34 and 2.20 J/g for 3, 5 and 10% (w/w) gelatin solutions respectively, indicating whey-egelatin interaction. Chicken skin gelatin gels exhibited a fine network whereas whey protein gels comprised aggregates and mixtures led to phase separation. This unutilized non-mammalian gelatin may lead to novel industrial applications. (C) 2014 Elsevier Ltd. All rights reserved.
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