## 3 Results and Discussion
### Thermal Treatment Parameters Optimization
In contrast, overheating at 100 \({}^{\circ}\)C results in a decrease in pepsin sensitivity, as indicated by an increase in the Michaelis constant (Km value) during digestion. However, overheating also prompts the production of new peptides with longer sequences, possibly due to the formation of irregular myosin aggregates [44]. The investigation into collagen denaturation in goose breast fillets revealed analogous associations to those observed for myosin denaturation. The analysis underscored that temperature, humidity, and fan rotation speed significantly impacted collagen denaturation in linear terms (\(p\leq 0.001\), \(p\leq 0.001\), \(p\leq 0.05\), respectively). However, the interactions between temperature \(\times\) fan rotation, temperature \(\times\) humidity, and humidity \(\times\) fan rotation speed did not yield statistically significant effects on collagen denaturation during the computer simulation (\(p>0.05\)). In addition, temperature exhibited a significant effect \begin{table}
\begin{tabular}{c c c c c} \hline \hline \multirow{2}{*}{**Factor**} & **Myosin Denaturation Level [\%]** & **Collagen Denaturation Level [\%]** & **Actin Denaturation Level [\%]** & **Cooking Loss [\%]** \\ \hline Intercept & 97.30 & 87.52 & 19.20 & 21.35 \\ Temp & 2.74 *** & 16.96 *** & 23.68 *** & 3.31 *** \\ Hum & 2.41 *** & 3.75 *** & 5.69 *** & 0.31 \\ Fan & 0.75 & 1.76 * & 3.81 *** & 1.59 \\ Temp \(\times\) Hum & \(-\)2.40 ** & \(-\)1.35 & 2.27 ** & \(-\)0.38 \\ Temp \(\times\) Fan & \(-\)0.70 & \(-\)0.95 & 2.92 *** & \(-\)0.23 \\ Hum \(\times\) Fan & \(-\)0.35 & \(-\)0.28 & \(-\)3.15 *** & 0.16 \\ Temp\({}^{2}\) & \(-\)0.49 & \(-\)8.11 *** & 25.91 *** & 0.14 \\ Hum\({}^{2}\) & \(-\)0.24 & 1.04 & \(-\)0.94 & 0.34 \\ Fan\({}^{2}\) & 0.66 & 0.59 & 0.2636 & \(-\)0.45 \\ R\({}^{2}\) & 0.922 & 0.982 & 0.997 & 0.758 \\ Lack of fit & 0.237 & 0.228 & 0.158 & 0.139 \\ \hline \hline \end{tabular}
\end{table} 
Table 2: Regression coefficients of the predicted quadratic polynomial models for the physical properties of myosin, collagen, actin denaturation, and cooking loss. on the extent of collagen denaturation in quadratic terms (\(p\leq 0.001\)). Conversely, humidity and air movement speed in the oven chamber did not demonstrate statistically significant quadratic effects on collagen denaturation (\(p>0.05\)). Research by [PERSON] and [PERSON] [38] focuses on comprehending how the collagen attributes of intermuscular connective tissue (IMCT) contribute to hardness and elasticity in various parts of meat after the cooking process. This work proposes a laboratory test of changes in IMCT after thermal treatment. The study involving thermal treatment (1 h) at varying temperatures (25\(-\)65 \({}^{\circ}\)C) was aimed at examining the chemical, mechanical, and thermal characteristics of collagen within the isolated IMCT-perimysium. The degree of collagen degradation, solubility of collagen components and proteoglycans, thermal properties, and mechanical stress were investigated on IMCT-treated perimysium. The results showed that collagen degradation significantly increased at 65 \({}^{\circ}\)C. The soluble proteoglycan fraction showed no change between treatments. The thermal properties showed significant changes at 65 \({}^{\circ}\)C. Denaturation enthalpies (\(\Delta\)H) increased, and denaturation peak temperature (T\({}_{\text{P}}\)) decreased relative to lower thermal treatments. Finally, there were no significant differences in mechanical properties and loading stresses between treatments. Degradation at 65 \({}^{\circ}\)C may indicate chemical changes in total collagen; labile populations were dissolved, while the stable population remained in the IMCT-perimysium. The effects of thermal treatment at higher temperatures and the presence of meat enzymes should be investigated in the future [45]. Research by [PERSON] [46] focuses on understanding differences in the amount and thermal stability of collagen in IMCT, which play a role in the differential elasticity of heat-treated meat.