Analysis of Changes in Protein Secondary Structure during Thermal Beef Processing by Two-Dimensional Correlated Infrared Spectroscopy
XIE Anguo, WANG Tingmin, ZHANG Qinhua, LI Chao, WANG Mansheng
1. Zhang Zhongjing School of Chinese Medicine, Nanyang Institute of Technology, Nanyang 473004, China; 2. Sichuan Manwei Longchu Biotechnology Co. Ltd., Meishan 620000, China; 3. Institute of Bast Fiber Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China
Abstract：This study used Fourier transform infrared (FTIR) spectroscopy and near-infrared (NIR) spectroscopy to analyze 66 beef samples heated for 0–15 min at 60 to 120 ℃, and revealed the dynamic evolution of protein structure by twodimensional correlation spectroscopy (2D-CoS). The results showed that as the heating temperature increased, the absorption peaks of amide A and amide I bands shifted, and the N–H and C–N vibrations increased. Moreover, the relative content of β-sheet increased and the relative content of β-turn decreased. The sequence of changes in the secondary structure of proteins was β-turn, β-sheet, α-helix and random coil. In addition, a predictive model for protein secondary structure (α-helix, β-sheet, β-turn and random coil) contents was constructed based on NIR spectroscopy data, which was demonstrated to have high predictive ability (corrected correlation coefficient > 0.9). In conclusion, this study provides an effective technical approach for fast structural analysis of proteins in meat products without the need for complex sample pretreatment.
谢安国，王廷敏，张芹华，李 超，王满生. 二维相关红外光谱技术解析牛肉热加工过程中蛋白质二级结构变化[J]. 肉类研究, 2024, 38(8): 1-7.
XIE Anguo, WANG Tingmin, ZHANG Qinhua, LI Chao, WANG Mansheng. Analysis of Changes in Protein Secondary Structure during Thermal Beef Processing by Two-Dimensional Correlated Infrared Spectroscopy. Meat Research, 2024, 38(8): 1-7.
2024, Vol. 38 
