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

Autor: M. Teresa Díaz, Helena M. Moreno, Mercedes M. Pedrosa, Fátima Domínguez-Timón, A. Javier Borderías, Clara A. Tovar
Přispěvatelé: Ministerio de Economía y Competitividad (España)
Rok vydání: 2020
Předmět:
Zdroj: Digital.CSIC. Repositorio Institucional del CSIC
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Popis: The 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.
This work was supported by the Spanish Ministry of Economy and Competitiveness (RTA2015-00003-C02).
Databáze: OpenAIRE