Effect of globular pea proteins fractionation on their heat-induced aggregation and acid cold-set gelation

By Jean-luc Mession, M. Chihi, Nicolas Sok, R. Saurel. 2015

202 citations recorded by the source corpus.

Subfields: Food Science, Plant Science

View Paper: https://www.semanticscholar.org/paper/cbf827bb7bc4f618302c20021fc5e89178b0b15b

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Citations in the corpus

• Pea protein isolates: Structure, extraction, and functionality (2018, background): “Due to its extensive quaternary structure and disulfide bridges, legumin has a more rigid conformation compared to vicilin.((90)) Accordingly, isolated vicilin fractions have demonstrated better functional behaviors than isolated legumin and mixed globulin fractions.”