## 3 Results and Discussion
### Texture Profile Analysis  
A TPA of Bologna-style sausages heated via OH and COV revealed that OH-treated samples generally had a less hard texture, with less capability to spring back to their original shape. This is reflected in significantly lower hardness and springiness values, respectively, as shown in Table 2. [PERSON] et al. also describe lower springiness values for OH-treated meat emulsion batters, whereas a comparable hardness to COV-treated samples was determined [11]. In contrast, [PERSON] et al. measured a lower hardness of Bologna-style sausages heated via OH [12], which is in accordance with results from this study. Further attributes that were significantly lower for OH-treated samples in this study are gumminess and chewiness, which is in line with the generally lower hardness of the product. Thus, less force needs to be applied when simulating the chewing process of OH-treated samples compared to COV-treated samples. The lower hardness of OH-treated samples is mainly ascribed to two reasons: (i) a decreased heating time when heated via OH and (ii) lower intermolecular interactions within the OH-treated sausage gel network. With regard to (i), aggregation and the formation of gel network structures in meat emulsion sausages start at temperatures surpassing 40 \({}^{\circ}\)C [44]. As shown in Figure 2a, the duration that samples were above 40 \({}^{\circ}\)C during OH is significantly lower compared to COV samples. In turn, OH-treated samples had a longer holding time after reaching the final temperature of 76 \({}^{\circ}\)C (i.e., 5 min for OH and 2 min for COV). However, the prolonged holding time at the final temperature did not lead to a similar hardness of the OH samples compared to the COV-treated samples. A shorter total treatment time, as applied in this study, leads to a lower total thermal energy input. Thus, less energy is available for protein denaturation besides the overall heating of the sample [45]. Less denaturation of a protein molecule is described as a less reactive state for protein-protein interactions and hence for aggregation and the subsequent formation of gel network structures [46]. Thus, a lower total thermal energy input due to shorter durations at denaturation temperatures reduces the likelihood of intermolecular interactions, e.g., hydrophobic interactions, which help stabilize a dense protein gel network. With regard to (ii), besides a lower total energy input, OH has also been demonstrated to decrease protein denaturation and aggregation or the formation of gel network structures due to non-thermal effects [37; 38; 39; 40; 41]. These effects are described, e.g., as a diverging motion of protein molecules due to interactions with the electric field [47]. At electrical frequencies in the kilohertz range, an oscillating motion of molecules is likely, as described by [PERSON] and [PERSON] [17]. This oscillating motion can lead to a constant reorientation of hydrophobic clusters, as described by [PERSON] et al. [37]. Furthermore, the oscillatory motion at kilohertz frequencies can reduce the rotational motion of the proteins, leading to a local restriction in dependence on the frequency applied [17; 48]. Thus, the possibility of physical interactions between proteins (e.g., via hydrophobic interactions) can be decreased due to non-thermal effects, which also negatively affect the sample's hardness when heated via OH. Besides hydrophobic interactions, disulfide bonds also play a crucial role in forming the gel network structures of meat emulsion batters, as they enhance the gel's hardness [44]. According to the literature, OH can reduce the number of disulfide bonds in these gel structures [39]. Therefore, we assume that the number of disulfide bonds in the OH-treated