## 3 Results and Discussion
### Myofibrillar Proteins
#### 3.1.6 Rheological Properties  
Rheological behavior alterations were used to analyze the correlations from the shifting to the MP gel network of MP [9]. The storage modulus (G') represents elastic solid behavior and can reflect mechanical strength, while the loss modulus (G\") represents the fluid viscosity ratio. Figure 5 showed the effect of OVA/\(\beta\)CD treatments on MPs rheological properties (G' and G\") after 90 days of frozen storage. All samples proved that the G' values dropped sharply from 35 to 45 \({}^{\circ}\)C, then gradually increased, decreased slightly at 53 \({}^{\circ}\)C, and subsequently increased. These two peaks are attributed to the higher activity of protease enzymes that degrade myosin, resulting in the breakage of gel strength, or the  
Figure 4: Circular dichroism of myofibrillar protein treated with different concentrations of OVA/\(\beta\)CD during 90 days of frozen storage at \(-18\) \({}^{\circ}\)C. (**A**) 0% OVA/\(\beta\)CD treatment. (**B**) 2% OVA/\(\beta\)CD treatment. (**C**) 4% OVA/\(\beta\)CD treatment. (**D**) 6% OVA/\(\beta\)CD treatment.  
conformational change of myosin disrupting the integrity of the protein network. The initial decline might be explained by partial MP degradation in the gel, which was attributed to the denaturation of myosin. A slight drop occurred at 55 \({}^{\circ}\)C; this sudden drop might be due to the deterioration of the myosin rod sub-fragmentation and the destruction of the temporary protein network during the heating process of the MPs. The subsequent rise may be explained by the establishment of a more stable gel network through protein-protein cross-linking [36]. The MPs treated with 6% OVA/\(\beta\)CD had higher G' values than the MPs treated with 2% and 4%, indicating that 6% treatment showed better MP gel stability. These results can be related to the disulfide bonds formed in myosin, which resulted in lower gel properties.  
Owing to the viscoelastic properties of MP gel, the thermal gel performance of MPs can be monitored by the G\" values. The change in the trend of G\" is roughly similar to that of G'. It started to decrease until temperature reached 47 \({}^{\circ}\)C, and then gradually increased until temperature reached 65 \({}^{\circ}\)C, after which it finally decreased. The final decline might have been due to the increase in the heat denaturation of the MPs, caused by the formation of protein-protein bonds that were surpassed by the destruction of the protein-protein, resulted in a decrease in G\". The values of G' and G\" tended to increase gradually as the OVA/\(\beta\)CD concentrations increased, indicating that the addition of OVA/\(\beta\)CD improved the strength of the gel network and made that gel network structure more stable and elastic [37]. Thence, from the above-mentioned results it can be confirmed that OVA/\(\beta\)CD contributed to a stronger gelation process. These conclusions are similar to the previously reported work indicating that cryoprotectant interaction with MPs produced gel networks with viscoelastic properties, which improved the gelation performance of the MP gels [19].  
Figure 5: _Cont._