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OA北大核心CSTPCD

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 two-dimensional 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.