1. National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China 2. Institute of Food Science, Jishou University, Jishou 416000, China 3. College of Food Science, Tibet Agricultural and Animal Husbandry College, Linzhi 860000, China
Abstract:The effect of S-configuration transformation on the microstructure of ovalbumin was studied by CD spectra, XRD spectra, ANS fluorescence probe emission spectra and UV absorption spectra. CD spectra was used to examine the changes in the secondary structure of the ovalbumin during S-ovalbumin information process. When the induction time was prolonged, the mutual transformation between α-helix, β-sheet, β-turn and the random coil was observed, and the orderliness of the secondary structure was increased with α-helix decreasing slightly and β-sheet increasing correspondingly. XRD spectra analysis showed that the crystal structure content of the ovalbumin increased with prolonging the induction time and the largest data was observed at 72 h, indicating that the orderliness of the secondary structure was increased. The results were similar to CD spectra analysis. The ANS fluorescence probe emission spectra analysis demonstrated that S-configuration transformation induced an increase in surface hydrophobicity with prolonging the induction time, and the largest data was also observed at 72 h. In addition, UV absorption spectra analysis indicated that S-configuration transformation resulted in a decrease in the UV-absorption maximum value with prolonging the induction time, indicating that the aromatic amino acid was buried in the molecular interior. The results indicated that the changes in the microstructure of ovalbumin were relevant to S-configuration transformation.
[1] Mine Y. Journal of Agricultural and Food Chemistry, 1997, 45: 2924. [2] Donvan J W, Mapes C J. Journal of the Science of Food and Agriculture, 1976, 27: 197. [3] Masayuki Yamasaki, Nobuyuki Takahashi, Masaaki Hirose. Journal of Biological Chenistry, 2003, 37: 35524. [4] Hammersh M, Larsen L B, Andersen A B. Lebensm. Technol., 2002, 35: 62. [5] Castellano A C, Barteri Binconi A, et al. Zeitschrift für Naturforschung, 1996, 51: 379. [6] Huntington J A, Patston P A, Ettins P G W. Protein Science, 1995, 4: 613. [7] Lucisano M, Hidalgo Comelli E M. Journal of Agricultural and Food Chemistry, 1996, 44: 1235. [8] Takahasn T, Atsumi E, Orita T. Bioscience Biotechnology and Biochemistry, 1996, 60: 1464. [9] Jolan de Groot, Hans A. Biotechnology and Bioengineering, 2007, 97(4): 475. [10] Smith M,Back B. Australian Journal of Biological Science, 1965, (18):365. [11] Hammersh M, Larsen L B, Qvist K B. Journal of Texture Studies, 2001, (32): 105. [12] Chang Y, Chen T C,Lang. International Journal of Food Properties, 1999, (49): 2001. [13] Jolan de Groot, Harmen H J, De Jongh. Protein Engineering, 2003, 16(12): 1035. [14] Egelndal B. Journal of Food Science, 1980, 45: 570. [15] YANG Xin-ping(杨新萍). Journal of Shanxi Normal University(Natural Science Edition)(山西师范大学学报·自然科学版), 2007, 21(1): 72. [16] Stein P E, Leslie A G, Finch J T, et al. J. Mol. Biol., 1991, 221: 941. [17] YE Huai-yi, YANG Su-ling, XU Qian(叶怀义, 杨素玲, 徐 倩). Journal of the Chinese Cereals and Oils Association(中国粮油学报), 2000, 15(6): 24. [18] Stefania Iametti, Elena Donnizzelli, Giuseppe Vecchio, et al. J. Agric. Food Chem., 1998, 46(9): 3521. [19] Zhang Hongkang, Li Lite, Tat Sumi Eizo, et al. Innovative Food Science and Energing Technologies, 2003, 4(3): 269. [20] CHEN Zhen-zhen, ZHANG Ning, ZHANG Wen-shen, et al(陈蓁蓁, 张 宁, 张文申, 等) . Chinese J. of Anal. Chem.(分析化学), 2006, 34(9): 134. [21] WU Dan, XU Gui-ying(吴 丹, 徐桂英). Acta Phys-Chim. Sin.(物理化学学报), 2006, 22(2): 254.