Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures

Renata Silva Diniz; Jane Sélia Dos Reis Coimbra; Álvaro Vianna Novaes de Carvalho Teixeira; Angélica Ribeiro da Costa; Igor José Boggione Santos; Gustavo Costa Bressan; Antonio Manuel da Cruz Rodrigues; Luiza Helena Meller da Silva

doi:10.1016/j.foodres.2014.05.079

Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures

Food Res Int. 2014 Oct:64:157-165. doi: 10.1016/j.foodres.2014.05.079. Epub 2014 Jun 17.

Authors

Renata Silva Diniz¹, Jane Sélia Dos Reis Coimbra², Álvaro Vianna Novaes de Carvalho Teixeira³, Angélica Ribeiro da Costa⁴, Igor José Boggione Santos⁴, Gustavo Costa Bressan⁵, Antonio Manuel da Cruz Rodrigues¹, Luiza Helena Meller da Silva¹

Affiliations

¹ Faculdade de Engenharia de Alimentos, Instituto de Tecnologia, Universidade Federal do Pará, Campus do Guamá 66000-000, Belém, PA, Brazil.
² Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa, Campus Universitário s/n, Centro, 36570-000, Viçosa, MG, Brazil. Electronic address: jcoimbra@ufv.br.
³ Departamento de Física, Universidade Federal de Viçosa, Campus Universitário s/n, Centro, 36570-000, Viçosa, MG, Brazil.
⁴ Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa, Campus Universitário s/n, Centro, 36570-000, Viçosa, MG, Brazil.
⁵ Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Campus Universitário s/n, Centro, 36570-000, Viçosa, MG, Brazil.

PMID: 30011635
DOI: 10.1016/j.foodres.2014.05.079

Abstract

The study of protein interactions has generated great interest in the food industry. Therefore, research on new supramolecular structures shows promise. Supramolecular structures of the whey proteins α-lactalbumin and glycomacropeptide were produced under varying heat treatments (25 to 75°C) and acidic conditions (pH3.5 to 6.5). Isothermal titration calorimetry experiments showed protein interactions and demonstrated that this is an enthalpically driven process. Supramolecular protein structures in aqueous solutions were characterized by circular dichroism and intrinsic fluorescence spectroscopy. Additional photon correlation spectroscopy experiments showed that the size distribution of the structures ranged from 4 to 3545nm among the different conditions. At higher temperatures, lower pH increased particle size. The foamability of the supramolecular protein structures was evaluated. Analysis of variance and analysis of regression for foaming properties indicated that the two-factor interactions between pH and temperature exhibited a significant effect on the volume and stability of the foam.

Keywords: Acidification; Calorimetry; Heating; Self-assembly; Techno-functional properties.