Moreno Conde, Helena MaríaDomínguez-Timón, FátimaDíaz Díaz Chirón, María TeresaPedrosa, MercedesBorderías, JavierTovar, Clara2024-02-012024-02-012020Moreno, Helena M., et al. «Evaluation of Gels Made with Different Commercial Pea Protein Isolate: Rheological, Structural and Functional Properties». Food Hydrocolloids, vol. 99, febrero de 2020, p. 105375. https://doi.org/10.1016/j.foodhyd.2019.105375.0268-005X10.1016/j.foodhyd.2019.105375https://hdl.handle.net/20.500.14352/97990The gelling of two commercial pea protein isolates (PPI) at 20% and 23% PPI concentration, and the effect of microbial transglutaminase (-0- and -5- U/g protein), were analysed. The final aim was to get PPI gels with textural properties enough to make meat and seafood analogues. The first PPI (-A-), was made by alkaline solubilization and isoelectric precipitation from pea flour. The second one (-B-), was obtained by aqueous dispersion of the pea flour and concentration of the soluble protein. The water and oil holding capacities of PPI-A suggested a higher degree of protein denaturation which was assessed by Dynamic thermo mechanical analysis (DMTA) and Fourier transform infrared spectroscopy (FTIR). FTIR data showed lower intermolecular β-sheet aggregates in PPI-B gels than in PPI-A. This result was consistent with the reticulated and well-interconnected network from scanning electron microscopy (SEM) of PPI-B gels in line with the higher strain amplitude (γmax), and the lower loss factor (tanδ) in PPI-B gels vs PPI-A gels. The MTGase enzyme significantly improved the structural quality of the PPI-B gels (high Q-factor) at 20% and 23% PPI. For all these reasons PPI B is more suitable for achieving consistent gels as bases for meat and seafood analogues.engAttribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/Evaluation of gels made with different commercial pea protein isolate: Rheological, structural and functional propertiesjournal article1873-7137https://doi.org/10.1016/j.foodhyd.2019.105375restricted accessPea protein isolateTransglutaminaseViscoelasticityCohesivenessCiencias BiomédicasVeterinaria33 Ciencias Tecnológicas