Evaluation of key aroma compounds and protein secondary structure in the roasted Tan mutton during the traditional charcoal process

Abstract

The traditional charcoal technique was used to determine the changes in the key aroma compounds of Tan mutton during the roasting process. The results showed that the samples at the different roasting time were distinguished using GC-MS in combination with PLS-DA. A total of 26 volatile compounds were identified, among which 14 compounds, including (E)-2-octenal, 1-heptanol, hexanal, 1-hexanol, heptanal, 1-octen-3-ol, 1-pentanol, (E)-2-nonenal, octanal, 2-undecenal, nonanal, pentanal, 2-pentylfuran and 2-methypyrazine, were confirmed as key aroma compounds through the odor activity values (OAV) and aroma recombination experiments. The OAV and contribution rate of the 14 key aroma compounds were maintained at high levels, and nonanal had the highest OAV (322.34) and contribution rate (27.74%) in the samples after roasting for 10 min. The content of α-helix significantly decreased (P < 0.05), while the β-sheet content significantly increased (P < 0.05) during the roasting process. The content of random coils significantly increased in the samples roasted for 0–8 min (P < 0.05), and then no obvious change was observed. At the same time, β-turn content had no obvious change. Correlation analysis showed that the 14 key aroma compounds were all positively correlated with the content of α-helix and negatively correlated with the contents of β-sheet and random coil, and also positively correlated with the content of β-turn, except hexanal and 2-methypyrazine. The results are helpful to promoting the industrialization of roasted Tan mutton.

Effect of Soy Wax/Rice Bran Oil Oleogel Replacement on the Properties of Whole Wheat Cookie Dough and Cookies

“…All the samples had β-turn and β-sheet, but only a select number of samples showed α -helix and random coil (Figure 6c). Recent studies have reported that α -helix and β-sheet are the most stable secondary structures, whereas β-turn and random coil indicated a more flexible protein structure [41]. D-0 and D-100 samples exclusively displayed α -helix structures and have high AUC for β-sheet, suggesting the protein network in these samples is more stable than in others.…”