## 3 Results and Discussion
### Viscoelastic Behavior of CPC-Stabilized Emulsions
#### 3.3.1 Emulsions Stabilized by Gelling CPC  
The CPC\({}_{\text{g}}\)-stabilized emulsions and CPC\({}_{\text{g}}\) dispersion at 20 \({}^{\circ}\)C behaved as free-flowing viscous liquids, where G\({}^{\prime\prime}\) was greater than G\({}^{\prime}\), and both moduli remained steady at constant temperature (Figure 2). To initiate the heat-induced gelation process in eC\({}_{\text{g}}\) the temperature was increased from 20 \({}^{\circ}\)C to 95 \({}^{\circ}\)C at a rate of 4 \({}^{\circ}\)C/min. Initially, both G\({}^{\prime}\) and G\({}^{\prime\prime}\) began to decrease as the overall viscosity of the emulsion decreased with increasing temperature. However, when the temperature reached \(\sim\)72 \({}^{\circ}\)C (after approx. 12 min of heating), both G\({}^{\prime}\) and G\({}^{\prime\prime}\) began to increase rapidly (Figure 2b). Such an increase in moduli values may suggest that the observed rheological behavior was directly related to the denaturation of the chickpea protein molecules. As a result of heat treatment (at 95 \({}^{\circ}\)C for 15 min), their globular conformation was irreversibly changed to a more random structure by exposure to previously buried hydrophobic groups leading to protein aggregation. [PERSON] et al. [58] indicated the presence of a broad denaturation peak in the range of \(\sim\)65-100 \({}^{\circ}\)C with a maximum at 90 \({}^{\circ}\)C on the DSC thermogram of an unhydrolyzed chickpea protein isolate. [PERSON] et al. [14] reported broad endothermic transition in the DSC scans of three chickpea protein isolates (20% \(w/v\) protein dispersion, pH 7) with the onset around 78-80 \({}^{\circ}\)C or 57 \({}^{\circ}\)C and the peak denaturation temperature values of 97-103 \({}^{\circ}\)C or 92 \({}^{\circ}\)C, respectively, depending on the method applied for their preparation. According to the authors, endothermic troughs in DSC thermograms were the result of overlapping thermal denaturation events of legumin and victim proteins in the former and those of the albumin fraction in the latter. It can be stated that the slight increase in G\({}^{\prime}\) and G\({}^{\prime\prime}\) around 55 \({}^{\circ}\)C could be attributed to the beginning of conformational changes for albumin fraction as a result of heating. Once the temperature reached 95 \({}^{\circ}\)C, G\({}^{\prime}\) was now significantly greater than G\({}^{\prime\prime}\) (i.e., a crossover was observed at 86 \({}^{\circ}\)C), indicating that the emulsion had transformed from a liquid into a solid-like state during the increasing temperature ramp. Then, during the isothermal hold step at 95 \({}^{\circ}\)C (17-32 min), G\({}^{\prime}\) and G\({}^{\prime\prime}\) continued to increase even though the temperature remained constant; however, G\({}^{\prime}\) began to increase at a slower rate during the second half of the isothermal hold at 95 \({}^{\circ}\)C. The increase in G\({}^{\prime}\) during gelation can be attributed to the formation of filamentous or fine-stranded aggregates. Previous studies have shown that (1) prolonged heating at 90 \({}^{\circ}\)C not only accelerates protein aggregation  
Figure 2: Elastic modulus (G\({}^{\prime}\)) and viscous modulus (G\({}^{\prime\prime}\)) plotted vs. time for CPC\({}_{\rm g}\) dispersion (C\({}_{\rm g}\)) (a), CPC\({}_{\rm g}\)-stabilized emulsion (eC\({}_{\rm g}\)) (b), and CPC\({}_{\rm g}\)-stabilized emulsion with 0.1M NaCl (eC\({}_{\rm g}\)N) (c) during the temperature ramp-up, hold, and ramp-down procedure. rates but also leads to the rapid formation of firmly structured gels and an overall more elastic gel network [59; 60]; (2) gelation of globular proteins at low ionic strength and pJ! pH! pH! pI produces fine-stranded gel [61]. Then, as the temperature was decreased back to 20 \({}^{\circ}\)C, both G\({}^{\prime}\) and G\({}^{\prime\prime}\) began to decrease rapidly.