@article{XIE2024, 
author = {Anguo XIE and Tingmin WANG and Qinhua ZHANG and Chao LI and Mansheng WANG},
title = {Analysis of Changes in Protein Secondary Structure during Thermal Beef Processing by Two-Dimensional Correlated Infrared Spectroscopy},
year = {2024},
journal = {Meat Research},
volume = {38},
number = {8},
pages = {1-7},
keywords = {beef, heating, secondary structure, two-dimensional correlation spectroscopy, near infrared spectroscopy},
url = {https://www.sciopen.com/article/10.7506/rlyj1001-8123-20240527-127},
doi = {10.7506/rlyj1001-8123-20240527-127},
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.}
}