## 3 Results and Discussion
### Oscillatory Dynamic Rheology
The G\" followed the same trend as the G', but the degree of ordered interaction was significantly stronger, resulting in a lower G\" value, showing that the elastic composition was the most important factor in surimi gel production. The G\" rose until it reached 38 \({}^{\circ}\)C, then dropped quickly to its lowest point at 48 \({}^{\circ}\)C. Following that, G\" climbed steadily up to 65 \({}^{\circ}\)C before dropping due to cross-linking [42]. Because G' values were higher than G\" values, the tan \(\delta\) of all samples was less than 1.0. As a result, all of the samples behaved like an elastic fluid with improved gelation properties [40]. The tan \(\delta\) represents the distribution of \"viscosity\" relative to \"elasticity\", which is shown by a pure solid at 0\({}^{\circ}\) and a pure liquid at 90\({}^{\circ}\)[43]. All surimi samples had a first peak at around 36 \({}^{\circ}\)C, as shown in Figure 2c. The unwashed sample, on the other hand, performed poorly in this temperature. The unfolding of the myosin structure at temperatures above 30 \({}^{\circ}\)C increased the viscosity of the sol [44]. Protein networks were generated as the temperature neared 42 \({}^{\circ}\)C (gel setting stage), as a result of the disulfide-linked heavy meromyosin, causing a drop in tan \(\delta\)[45]. Following that, the tan \(\delta\) rose rapidly up to 50 \({}^{\circ}\)C, which could be due to greater protein unfolding and interaction between unfolded proteins and water molecules at low temperatures (before 50 \({}^{\circ}\)C). The heavy meromyosin connected by a disulfide bond was broken by the unfolding of subfragment-2, therefore the tan \(\delta\) increased as the temperature climbed in the 44-50 \({}^{\circ}\)C range. Because the structural modification of myosin had already been performed and the protein structure rearranged, the disulfide linkages and hydrophobic interactions between the molecules were strengthened when the temperature was above 50 \({}^{\circ}\)C, resulting in increased rigidity and intensity, but weakened mobility. When the temperature reached above 50 \({}^{\circ}\)C, this might be used to explain why the tan \(\delta\) faded as the temperature rose [46]. The solgel transition (tan \(\delta\)) of washed mince from threadfin brex revealed three transition points, which occurred at 36.7, 43.3, and 70.0 \({}^{\circ}\)C, according to [PERSON] et al. [47]. The transitions at 36.7 and 43.3 \({}^{\circ}\)C referred to the myosin tail and the transition at the higher temperature referred to the myosin head [47]. Furthermore, it had depicted shifting of curves (G' and G\") and peaks (tan \(\delta\)) at around 50 \({}^{\circ}\)C in this study. When compared to the unwashed sample, this was shifted to the lowest temperature during the transition phase of the W3 sample, followed by W2 and W1. It could be a difference in concentration and function of myofibrillar proteins or interfered gelling components, as well as proteins' ability to entrap water in gel networks, which could be in accordance with the expressible drip of samples (see Section 3.4.2),  
Figure 2: Changes in dynamic viscoelastic behavior of unwashed minec (U) and surimi pastes from Indian mackerel prepared by one washing cycle (W1), two washing cycles (W2), and three washing cycles (W3). The rheograms show elastic modulus, G’ (**a**), viscous modulus, G” (**b**), and tan \(\delta\) (**c**). Samples were heated from 10 \({}^{\circ}\)C to 90 \({}^{\circ}\)C.  
resulting in interval changes in gel formation. According to [PERSON] and [PERSON] (2018), increasing the moisture content increased the denaturation temperature of fish proteins, and caused the gel formation to be delayed. Despite the fact that the final G' and G\" of surimi differed, the tan \(\delta\) was nearly same, indicating that all surimi will undergo the same degree of sol-gel transition after thermal gelation.