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| 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 |
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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.
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SUN Ge, WU Tongxuan, MAO Yanwei, LI Junling, ZHU Lixian, TONG Lin, ZHANG Xinjun, CHENG Haijian, GU Yue, ZHANG Yimin. Advances in Understanding the Mechanism of Red Meat Spoilage Caused by Bacteria[J]. Meat Research, 2024, 38(8): 63-71. |
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2024, Vol. 38 
