## 4 Discussion  
The consumption of high-quality proteins is of paramount importance for the maintenance of the skeletal muscle-to-total body weight ratio, as it stimulates the synthesis of muscle proteins ([PERSON] et al., 2019) [34]. The moisture, ash, crude protein, crude fat, and carbohydrate contents of DMP were approximately 4.7%, 4.9%, 68.9%, 7.7%, and 13.7%, respectively. The composition of DMH was found to be similar to that of DMP. However, the present study was limited in that it did not analyze the amino acid composition of DMP and DMH. In this study, the two enzymes were combined to create DMH, which has the potential to be used as a high-quality protein material. The present study revealed that DMP is comprised of a considerable proportion of proteins with a molecular weight below 15 kDa. Despite the utilisation of SDS-PAGE with increasing concentrations of acrylamide, proteins with a molecular weight below 15 kDa remained unidentified, indicating a potential limitation. However, the results of protein hydrolysis of DMH using SDS-PAGE demonstrated that alcalase and bromelain were effective in hydrolysing the polymeric proteins in DMP. Furthermore, the NPN content, an indicator used to assess protein hydrolysis, was quantified, and it was found that the NPN content of DMH was notably higher than that of DMP. Bromelain is a plant-derived proteolytic enzyme from the stem and juice of the pineapple plant (Ananas comosus) and is categorized as a cysteine endoprotease [28]. It has been reported that protein hydrolyses prepared using bromelain have the capacity to increase the content of low-molecular-weight peptides [35]. Alcalase is a microbial proteolytic enzyme derived from the fermentation of Bacillus licheniformis and is a serine endopeptidase that cleaves peptide bonds [36]. Alcalase is widely used for the production of bioactive peptides through the cleavage of peptide bonds located midway along the peptide chain [37]. Alcalase effectively hydrolyzes rice bran proteins, resulting in peptides with enhanced bioactivities [38]. The hydrolysis of proteins by enzymatic treatment can increase their digestibility by breaking down high-molecular-weight proteins into low-molecular-weight peptides [39]. Furthermore, [PERSON] et al. [40] reported that growing pigs fed a diet supplemented with mealworm hydrolysate exhibited enhanced protein digestibility compared with those receiving other supplements. DEX, a synthetic glucocorticoidoid, was used to induce damage in C2C12 cells by inhibiting protein synthesis and promoting protein degradation [41]. In the present study, treatment of C2C12 cells with 100 uM DEX resulted in cell damage and reduced cell viability. However, the viability of C2C12 cells was restored when DMH was added at a concentration of 5 mg/mL or higher, yielding results analogous to those observed by [PERSON] et al. [42]. These authors demonstrated that the addition of mealworm extract restored the viability of C2C12 cells after DEX-induced cell damage. DEX has also been employed in vivo to induce a reduction in muscle mass and strength in rats, as it activates the ubiquitin-proteasome system [43]. Furthermore, the administration of DEX intraperitoneally has been observed to induce weight loss in rats when the concentration exceeds a certain threshold. Based on the findings of preliminary experiments, the concentration of intraperitoneal DEX was set at 2.25 mg/kg. The results demonstrated that DEX administered intraperitoneally markedly reduced the body weight of rats, consistent with the observations reported by [PERSON] and [PERSON] [44], who used 2 mg/kg of DEX (i.p.) to induce weight loss in rats. A limitation of this study is that although dexamethasone administration intraperitoneally resulted in a transient reduction in body weight, it did not lead to a corresponding reduction in muscle mass in the rats. Although the muscle protein synthesis factors MyoD and myogenin were reduced in comparison to the control group, it is speculated that the duration of DEX (i.p.)