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- Estrada-Fernández, A.G.; Román-Guerrero, A.; Jiménez-Alvarado, R.; Lobato-Calleros, C.; Alvarez-Ramirez, J.; Vernon-Carter, E.J.
- Journal of food engineering 2018 v.221 pp. 35-44
- protein secondary structure, etc ; biopolymers; contact angle; droplet size; droplets; emulsions; hydrophobicity; oil-water interface; oils; pH; storage time; surface tension; surfactants; temperature; whey protein; Show all 15 Subjects
- ... Soluble (SC) and insoluble (IC) complexes were obtained from interacting whey protein concentrate-gum Arabic, at pH of 4.0, using biopolymer mass ratios of 2:1 and 3:1, respectively. Particles (SPT) were produced from IC and dried at different temperatures. Higher temperatures induced a higher contact angle, modified the protein secondary structure to a greater extent, and decreased the interfacia ...
- Mantovani, Raphaela Araujo; de Figueiredo Furtado, Guilherme; Netto, Flavia Maria; Cunha, Rosiane Lopes
- Journal of food engineering 2018 v.223 pp. 99-108
- protein secondary structure, etc ; dispersions; emulsifiers; emulsifying properties; emulsions; energy density; hydrophobicity; pH; surface tension; viscosity; whey protein isolate; Show all 11 Subjects
- ... The effect of pH and mechanical processes on non-heated whey protein isolate (WPI) and WPI fibril was evaluated from structural, physical and emulsifying properties. Fibril aggregation was observed increasing pH from 2 to 7 whilst mechanical processes with high energy density resulted in fibril shortening and smaller aggregates. Despite affecting fibril morphology, mechanical processes did not aff ...