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Evaluation of gels made with different commercial pea protein isolate: Rheological, structural and functional properties

AuthorsMoreno Conde, Helena María CSIC ORCID; Domínguez-Timón, Fátima; Díaz, M. Teresa; Pedrosa, Mercedes M.; Borderías, A. Javier CSIC ORCID ; Tovar, C. A.
KeywordsPea protein isolate
Issue Date2020
CitationFood Hydrocolloids 99: 105375 (2020)
AbstractThe 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.
Publisher version (URL)https://doi.org/10.1016/j.foodhyd.2019.105375
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