## 4 Conclusions  
Food processing may lead to changes in the structure and functionality of proteins. Understanding these changes is crucial when selecting protein powders for specific applications. The presented findings indicate that the type of chickpea concentrate used as an emulsion stabilizer (standard CPC and gelling CPC) has a significant impact on the stability and rheological behavior of the emulsion. Moreover, it determines the functionality of the protein-stabilized emulsion (e.g., its tendency to gel), particularly in combination with environmental conditions (heat- and/or salt treatment). The gelling CPC produced a fine, homogeneous emulsion with an average particle size \(<\) 1 \(\upmu\)m and Newtonian behavior that formed a heat-induced gel. However, gelation was accompanied by emulsion stabilization and a significant change in both shear rheological properties and particle size distribution, only in the presence of salt. The heat- (95 \({}^{\circ}\)C) and salt (0.1 M NaCl) treatment lead to the formation of a coarsely aggregated particulate gel. Emulsions stabilized with standard CPC (eC\({}_{\rm s}\)) were unstable non-Newtonian fluids due to large particle sizes. eC\({}_{\rm s}\) formed a thermoreversible viscoelastic structure during heat treatment. The addition of 0.1M NaCl improved the physical stability of the eC\({}_{\rm s}\) when it was accompanied by heat treatment; but in this case, no gel structure was formed. The selection of the protein powders and their processing conditions is of key importance, among others, in modeling functional food matrices, especially in the field of creating protein-based delivery systems for nutraceuticals. The following supporting information can be downloaded at [[https://www.mdpi.com/article/10.3390/app14072698/s1](https://www.mdpi.com/article/10.3390/app14072698/s1)]([https://www.mdpi.com/article/10.3390/app14072698/s1](https://www.mdpi.com/article/10.3390/app14072698/s1)), Figure S1: The PSD graphs (cumulative and histogram) for CPC\({}_{\rm s}\) and CPC\({}_{\rm g}\) dispersions (C\({}_{\rm s}\) and C\({}_{\rm g}\)), pre-processed once (\({}^{\rm one\ HPH}\)) or twice (\({}^{\rm two\ HPH}\)) in high-pressure two-stage homogenizer (a) and for corresponding emulsions, eC\({}_{\rm s}\) and eC\({}_{\rm g}\), obtained from these dispersions (b); Figure S2: The Turbiscan Stability Index (_TSI_) kinetics of global destabilization for CPC\({}_{\rm g}\)- and CPC\({}_{\rm s}\)-stabilized emulsion (a and b, respectively), where eC\({}_{\rm g}\) and eC\({}_{\rm s}\)--untreated samples; eC\({}_{\rm g}\)N and eC\({}_{\rm s}\)N--samples with 0.1 M NaCl; eC\({}_{\rm g}\)T and eC\({}_{\rm s}\)T--sample heated to 95 \({}^{\circ}\)C; eC\({}_{\rm g}\)NT and eC\({}_{\rm s}\)NT--samples with 0.1M NaCl heated to 95 \({}^{\circ}\)C; Figure S3: The PSD graphs (cumulative and histogram) for CPC\({}_{\rm g}\)- and CPC\({}_{\rm s}\)-stabilized emulsions (a and b, respectively), where eC\({}_{\rm g}\) and eC\({}_{\rm s}\)--untreated samples; eC\({}_{\rm g}\)N and eC\({}_{\rm s}\)N--samples with 0.1M NaCl; eC\({}_{\rm g}\)T and eC\({}_{\rm s}\)T--samples heated to 95 \({}^{\circ}\)C; eC\({}_{\rm g}\)NT and eC\({}_{\rm s}\)NT--samples with 0.1M NaCl heated to 95 \({}^{\circ}\)C; Figure S4: CLSM images of CPC\({}_{\rm g}\)-stabilized emulsions (a-c) and CPC\({}_{\rm s}\)-stabilized emulsions (d-f), where (a,d) untreated emulsions; (b,e) emulsions heated to 95 \({}^{\circ}\)C; (c,f) emulsions with 0.1 M NaCl heated to 95 \({}^{\circ}\)C. The green regions represent lipids and blue means the protein.