TY - JOUR
T1 - Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques
AU - Batista, A. P.
AU - Portugal, Carla A. M.
AU - Sousa, Isabel
AU - Crespo, João G.
AU - Raymundo, Anabela
N1 - This work is part of the research project “ Vegetable proteins in foods as an alternative to dairy desserts ” sponsored by Fundação para a Ciência e a Tecnologia (Reference POCTI/AGR/38251/2001) and CIERT of Instituto Piaget. Carla A.M. Portugal acknowledges the research grant PRAXIS XXI/BD/19817/99 from Fundação para a Ciência e a Tecnologia. The authors acknowledge Eng. Cristiana Nunes (CERTA - Instituto Piaget de Mirandela) for technical support and Professor António Maçanita for the access to the spectrofluorometer used for fluorescence anisotropy measurements.
PY - 2005/8/1
Y1 - 2005/8/1
N2 - 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.
AB - 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.
KW - Fluorescence anisotropy
KW - Gels
KW - Intrinsic viscosity
KW - Rheology
KW - Steady-state fluorescence
KW - Vegetable proteins
UR - http://www.scopus.com/inward/record.url?scp=23044473689&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2005.04.003
DO - 10.1016/j.ijbiomac.2005.04.003
M3 - Article
C2 - 15996729
AN - SCOPUS:23044473689
VL - 36
SP - 135
EP - 143
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
IS - 3
ER -