The effect of protein concentration and heat treatment temperature on micellar casein-soy protein mixtures

被引:87
作者
Beliciu, Cosmin M. [1 ]
Moraru, Carmen I. [1 ]
机构
[1] Cornell Univ, Dept Food Sci, Ithaca, NY 14853 USA
关键词
Soy proteins; Micellar casein; Protein mixtures; Rheology; MAIZE STARCH SYSTEMS; WHEY PROTEINS; THERMAL-DENATURATION; RHEOLOGICAL PROPERTIES; SOYBEAN PROTEINS; PHASE-BEHAVIOR; KAPPA-CASEIN; MILK; STABILITY; AGGREGATION;
D O I
10.1016/j.foodhyd.2011.01.011
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The objective of this study was to investigate the effect of concentration and temperature on the rheological properties of soy proteins (SP) and micellar casein (MCN) systems. Individual and mixed (1: 1) protein systems of 2-15% concentration were prepared and heat treated for 5 min at 40-90 degrees C. After cooling to 20 degrees C, their rheological properties were determined using steady-shear rheology. Zeta potential and particle size measurements were also conducted. Both proteins were negatively charged under all experimental conditions, but the absolute values of zeta potential and thus the stability of the protein solutions decreased with temperature and concentration. For SP solutions, viscosity and apparent yield stress increased with concentration. Shear thinning behavior was prevalent, becoming more pronounced with increasing concentration. Heat treatments at T >= 80 degrees C induced glycinin denaturation, followed by aggregation and network formation when C >= 7.5%. Heat treatment did not significantly affect viscosity of MCN systems, while increasing concentration resulted in a significant increase in apparent viscosity and apparent yield stress. Most MCN systems exhibited Newtonian flow behavior, with the exception of systems with C >= 12.5% treated at T >= 80 degrees C, which became slightly shear thickening. Mixed SP-MCN systems mimicked the behavior of SP, with most values of rheological parameters intermediate between SP and MCN-only systems. Mixtures of 7.5-12.5% concentration treated at 90 degrees C displayed local phase separation, low viscosity and apparent yield stress, while 15% mixtures treated at 90 degrees C showed protein aggregation and incipient network formation. The data generated in this study can be used to develop a range of protein based products with unique flow characteristics and storage stability. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1448 / 1460
页数:13
相关论文
共 61 条
[1]  
Abdullah M., 2003, Pakistan Journal of Nutrition, V2, P305
[2]   zeta-Potentials of casein micelles from reconstituted skim milk heated at 120 degrees C [J].
Anema, SG ;
Klostermeyer, H .
INTERNATIONAL DAIRY JOURNAL, 1996, 6 (07) :673-687
[3]  
Anema SG, 1997, MILCHWISSENSCHAFT, V52, P217
[4]   Thermal aggregation of whey proteins in model solutions as affected by casein/whey protein ratios [J].
Beaulieu, M ;
Pouliot, Y ;
Pouliot, M .
JOURNAL OF FOOD SCIENCE, 1999, 64 (05) :776-780
[5]   Effect of solvent and temperature on the size distribution of casein micelles measured by dynamic light scattering [J].
Beliciu, C. M. ;
Moraru, C. I. .
JOURNAL OF DAIRY SCIENCE, 2009, 92 (05) :1829-1839
[6]   Reversible shear thickening in monodisperse and bidisperse colloidal dispersions [J].
Bender, J ;
Wagner, NJ .
JOURNAL OF RHEOLOGY, 1996, 40 (05) :899-916
[7]  
BIKBOW TM, 1979, POLYM BULL, V1, P865
[8]  
Biswas PK, 2002, J FOOD SCI TECH MYS, V39, P702
[9]  
BROCHARDWYART F, 1990, CR ACAD SCI II, V310, P1169
[10]  
Carr A.J., 2003, Advanced Dairy Chemistry Volume 1: Proteins, V1, P1289