Design of bio-based supramolecular structures through self-assembly of α-lactalbumin and lysozyme

• Published in: Food hydrocolloids Vol. 58; pp. 60 - 74
• Main Authors: Monteiro, Adenilson A., Monteiro, Márcia R., Pereira, Ricardo N., Diniz, Renata, Costa, Angélica R., Malcata, F. Xavier, Teixeira, José A., Teixeira, Álvaro V., Oliveira, Eduardo B., Coimbra, Jane S., Vicente, António A., Ramos, Óscar L.
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.07.2016
• Subjects: Assembly mechanism; calorimetry; cattle; chemical interactions; circular dichroism spectroscopy; Electrostatic interactions; fluorescence emission spectroscopy; Food application; Food-grade structures; Foods; Globular proteins; heat; heat treatment; Heating; hydrocolloids; isoelectric point; lactalbumin; light scattering; Lysozyme; Morphology; Proteins; Self assembly; temperature; Thermal treatment; titration; Transmission electron microscopy; Electrostatic interactions; Food application; Food-grade structures; Assembly mechanism; Globular proteins; Thermal treatment

Bovine α-lactalbumin (α-La) and lysozyme (Lys), two globular proteins with highly homologous tertiary structures and opposite isoelectric points, were used to produce bio-based supramolecular structures under various pH values (3, 7 and 11), temperatures (25, 50 and 75 °C) and times (15, 25 and 35 m...