Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques

被引:77
作者
Batista, AP
Portugal, CAM
Sousa, I
Crespo, JG
Raymundo, A [1 ]
机构
[1] CIEAB, Inst Piaget ISEIT Almada, P-2800305 Almada, Portugal
[2] Univ Nova Lisboa, Requimte Dept Quim, CQFB, Fac Ciencias & Tecnol, P-2829516 Caparica, Portugal
[3] Inst Super Agron, DAIAT, Seccao Ciencia & Tecnol Alimentos, P-1349017 Lisbon, Portugal
关键词
vegetable proteins; gels; intrinsic viscosity; rheology; steady-state fluorescence; fluorescence anisotropy;
D O I
10.1016/j.ijbiomac.2005.04.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:135 / 143
页数:9
相关论文
共 27 条
[1]  
Bollinger H., 2001, Food Marketing & Technology, V15, P10
[2]   Textural property of 6 legume curds in relation to their protein constituents [J].
Cai, R ;
McCurdy, A ;
Baik, BK .
JOURNAL OF FOOD SCIENCE, 2002, 67 (05) :1725-1730
[3]   PROTEIN GELS [J].
FERRY, JD .
ADVANCES IN PROTEIN CHEMISTRY, 1948, 4 :1-78
[4]   Influence of processing variables on the rheological and textural properties of lupin protein-stabilized emulsions [J].
Franco, JM ;
Raymundo, A ;
Sousa, I ;
Gallegos, C .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1998, 46 (08) :3109-3115
[5]   High pressure promotes beta-lactoglobulin aggregation through SH/S-S interchange reactions [J].
Funtenberger, S ;
Dumay, E ;
Cheftel, JC .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1997, 45 (03) :912-921
[6]   SOY PROTEIN GELATION [J].
HERMANSSON, AM .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 1986, 63 (05) :658-666
[7]  
Lakowicz J. R., 2006, Principles of Fluorescence Spectroscopy Springer
[8]   Confocal laser scanning microscopy and image analysis of kinetically trapped phase-separated gelatin/maltodextrin gels [J].
Lorén, N ;
Langton, M ;
Hermansson, AM .
FOOD HYDROCOLLOIDS, 1999, 13 (02) :185-198
[9]   Effect of thermal treatment and composition on the mechanical properties of pea/kappa-carrageenan/starch desserts [J].
Nunes, MC ;
Raymund, A ;
Sousa, I .
GUMS AND STABILIZERS FOR THE FOOD INDUSTRY 12, 2004, (294) :54-64
[10]   Vegetable proteins and milk puddings [J].
Nunes, MC ;
Batista, P ;
Raymundo, A ;
Alves, MM ;
Sousa, I .
COLLOIDS AND SURFACES B-BIOINTERFACES, 2003, 31 (1-4) :21-29