Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques.
This work aims to present a comprehensive study about the macroscopic characteristics of globular vegetable proteins, in terms of their gelling ability, by understanding their molecular behaviour, when submitted to a thermal gelling process. The gels of soy, pea and lupin proteins were characterized by rheological techniques. Gelation kinetics, mechanical spectra, as well as the texture of these gels were analyzed and compared. Additionally, capillary viscometry, steady-state fluorescence and fluorescence anisotropy were used to monitor the structural changes induced by the thermal denaturation, which constitutes the main condition for the formation of a gel structure. Based on these techniques it was possible to establish a relationship between the gelling ability of each protein isolate and their structural resistance to thermal unfolding, enabling us to explain the weakest and the strongest gelling ability observed for lupin and soy proteins isolates, respectively.
Batista
Ana Paula
AP
CIEAB, Instituto Piaget-ISEIT de Almada, Quinta da Arreinela de Cima, 2800-305 Almada, Portugal.
Portugal
Carla A M
CA
Sousa
Isabel
I
Crespo
João G
JG
Raymundo
Anabela
A
D016880:Anisotropy; D005916:Globulins / Q000737:chemistry; D006358:Hot Temperature; D007700:Kinetics; D031297:Lupinus; D046911:Macromolecular Substances / Q000737:chemistry; D018532:Pisum sativum / Q000378:metabolism; D014674:Plant Proteins, Dietary / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012212:Rheology; D030262:Soybean Proteins / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013499:Surface Properties; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors; D014675:Vegetables / Q000378:metabolism*
D005916:Globulins; D046911:Macromolecular Substances; D014674:Plant Proteins, Dietary; D011506:Proteins; D030262:Soybean Proteins