Spectroscopic Evaluation of Effects of Heat Treatments on the Structures and Emulsifying Properties of Caseins
ZHANG Hao1, WANG Peng-jie2, LEI Xin-gen3, YANG Hong-ju4, ZHANG Lu-da2, REN Fa-zheng2, ZHENG Li-min1*
1. College of Information and Electrical Engineering, China Agricultural University, Beijing 100094, China 2. Laboratory of Functional Dairy, China Agricultural University, Beijing 100094,China 3. Cornel University, NY 14456, USA 4. Quality Control and Inspection Center for Domestically Animal Products, Ministry of Agriculture, Beijing 100094, China
Spectroscopic Evaluation of Effects of Heat Treatments on the Structures and Emulsifying Properties of Caseins
ZHANG Hao1, WANG Peng-jie2, LEI Xin-gen3, YANG Hong-ju4, ZHANG Lu-da2, REN Fa-zheng2, ZHENG Li-min1*
1. College of Information and Electrical Engineering, China Agricultural University, Beijing 100094, China 2. Laboratory of Functional Dairy, China Agricultural University, Beijing 100094,China 3. Cornel University, NY 14456, USA 4. Quality Control and Inspection Center for Domestically Animal Products, Ministry of Agriculture, Beijing 100094, China
摘要: The effects of heat treatment (heating temperature and pH) on the structures and emulsifying properties of caseins were systematically studied by spectroscopy. Heat treatment from 60 to 100 ℃ resulted in an increase in their fluorescence intensity, hydrodynamic diameter, turbidity and emulsifying activity index, but decreased the size polydispersity of caseins. In the pH range of 5.5 to 7.0, the fluorescence intensity, hydrodynamic diameter, turbidity and emulsifying properties decreased with increased heating pH, but the size polydispersity of caseins increased with increased pH. The relationship between the surface fluorescence intensity and emulsifying activity was also investigated, revealing a correlation coefficient of 0.90. These results suggested that heat treatment could be used to modify the structures and emulsifying properties of caseins by appropriately selecting heating conditions.
Abstract:The effects of heat treatment (heating temperature and pH) on the structures and emulsifying properties of caseins were systematically studied by spectroscopy. Heat treatment from 60 to 100 ℃ resulted in an increase in their fluorescence intensity, hydrodynamic diameter, turbidity and emulsifying activity index, but decreased the size polydispersity of caseins. In the pH range of 5.5 to 7.0, the fluorescence intensity, hydrodynamic diameter, turbidity and emulsifying properties decreased with increased heating pH, but the size polydispersity of caseins increased with increased pH. The relationship between the surface fluorescence intensity and emulsifying activity was also investigated, revealing a correlation coefficient of 0.90. These results suggested that heat treatment could be used to modify the structures and emulsifying properties of caseins by appropriately selecting heating conditions.
ZHANG Hao1, WANG Peng-jie2, LEI Xin-gen3, YANG Hong-ju4, ZHANG Lu-da2, REN Fa-zheng2, ZHENG Li-min1* . Spectroscopic Evaluation of Effects of Heat Treatments on the Structures and Emulsifying Properties of Caseins [J]. 光谱学与光谱分析, 2013, 33(05): 1275-1280.
ZHANG Hao1, WANG Peng-jie2, LEI Xin-gen3, YANG Hong-ju4, ZHANG Lu-da2, REN Fa-zheng2, ZHENG Li-min1* . Spectroscopic Evaluation of Effects of Heat Treatments on the Structures and Emulsifying Properties of Caseins . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2013, 33(05): 1275-1280.
[1] Bu H, Hu Y, Sood S M,et al. Archives of Biochemistry and Biophysics, 2003, 415(2): 213. [2] Syme C D, Blanch E W, Holt C,et al. European Journal of Biochemistry, 2003, 269(1): 148. [3] Horne D S. Casein Micelle Structure and Stability. San Diego: Academic Press,2008. [4] Raikos V. Food Hydrocolloids, 2010, 24: 259. [5] Haskard C A, Li-Chan E C Y. Journal of Agricultural and Food Chemistry, 1998, 46(7): 2671. [6] Liu Y, Guo R. Biophysical Chemistry, 2008, 136(2-3): 67. [7] Beliciu C M, Moraru C I. Journal of Dairy Science, 2009, 92(5): 1829. [8] Janφj Th, Ipsen R. Milchwissenschaft, 2006, 61: 131. [9] Kamath S, Webb R E, Deeth H C. Journal of Dairy Science, 2011, 94(6): 2707. [10] Cuomo F, Ceglie A, Lopez F. Food Chemistry, 2011, 126(1): 8. [11] Trejo R, Harte F. Journal of Dairy Science, 2010, 93(6): 2338. [12] Anema S. Journal of Agricultural and Food Chemistry, 1998, 46(6): 2299. [13] Partschefeld C, Schwarzenbolz U, Richter S,et al. Biotechnol. J., 2007, 2(4): 456. [14] Gastaldi E, Lagaude A, Marchesseau S,et al. Journal of Food Science, 1997, 62(4): 671. [15] Wang X S, Tang C H, Li B S,et al. Food Hydrocolloids, 2008, 22(4): 560. [16] Lee S-Y, Morr C V, Ha E Y W. Journal of Food Science, 1992, 57(5): 1210. [17] Fox P F, Brodkorb A. International Dairy Journal, 2008, 18(7): 677. [18] Madadlou A, Mousavi M E, Emam-Djomeh Z,et al. Food Chemistry, 2009, 116(4): 929. [19] Martin G J O, Williams R P W, Dunstan D E. Journal of Dairy Science, 2007, 90(10): 4543. [20] López-fandio R. Critical Reviews in Food Science and Nutrition, 2006, 46(4): 351.