Wound healing incurs various challenges, making it an important topic in medicine. Short-chain peptides from fish protein hydrolysates possess wound healing properties that may represent a solution. In this study, perch hydrolysates were produced from perch side steams using a designed commercial complex enzyme via a proprietary pressure extraction technique. The average molecular weight of the perch peptides was 1289 kDa, and 62.60% of the peptides had a low molecular weight (≤1 kDa). Similarly to the beneficial amino acid sequence FPSIVGRP, FPSLVRGP accounted for 6.21% abundance may have a potential antihypertensive effect. The concentrations of collagen composition and branched-chain amino acids were 1183 and 1122 mg/100 g, respectively. In a fibroblast model, active perch peptides accelerated wound healing mainly by increasing the secretion of procollagen I, fibronectin, and hyaluronan. In an SD rat model established to mimic human wounds, orally administered perch hydrolysates with a molecular weight below 2.3 kDa accelerated wound healing, which mainly resulted from collagen-forming amino acids, branched-chain amino acids, and matrikine. Collectively, the residue of perch extract can be upcycled via a hydrolysis technique to produce not only bioactive sequences but also short-chain peptides. Considering the therapeutic potential to promote wound healing, such by-products are of great value and may be developed as dietary nutraceuticals.

Muscle atrophy, through several pathways including increased protein catabolism, leads to adverse effects in cachexia induced by cancer and chemotherapy. Perch essence (PE) is a perch extract rich in branched-chain amino acids and peptides. The present study initially investigated the effects of PE supplementation on muscle atrophy in a mouse model of cancer cachexia induced by C26 cancer cells and compared these effects with those of tryptone. Compared with the tumor-only group, we found that PE supplementation significantly improved body weight, muscle mass, maximum limb grip strength (MLGS), and myosin heavy chain expression in the muscles of tumor-bearing mice. PE also significantly inhibited the expression of factors related to protein degradation, oxidative stress, and inflammation, while enhancing the expression of antioxidant enzymes in tumor-bearing mice. These effects of PE were associated with an increased expression of phosphorylated Akt and forkhead box protein O1, along with a reduced expression of phosphorylated nuclear factor-κB p65 in the muscles of tumor-bearing mice. Furthermore, PE similarly increased MLGS and attenuated muscle atrophy in mice exposed to cisplatin by inhibiting protein degradation. All the therapeutic effects of PE supplementation mentioned above were generally greater than those of tryptone supplementation. These results suggest the potential of PE in protecting against muscle atrophy induced by tumors or chemotherapy.

Wound healing incurs various challenges, making it a paramount topic in medicine. Short chain peptides from fish protein hydrolysates pose wound healing properties that may bring a solution. In this study, perch hydrolysates were produced from perch side steams using a designed commercial complex enzyme via a proprietary pressure extraction technique. The average molecular weight of the perch peptides was 1,289 kDa, and 62.60% of the peptides had a low molecular weight (≤ 1 kDa). The beneficial amino acid sequence FPSLVRGP with antihypertensive effects accounted for 6.21% abundance. The concentrations of collagen composition and branched chain amino acids was 1183 and 1122 mg/100g, respectively. In fibroblast model, active perch peptides accelerated wound healing mainly by increasing the secretion of procollagen I, fibronectin, and hyaluronan. In SD rat model to mimic human wound, orally perch hydrolysates with a molecular weight below 2.3 kDa accelerating wound healing mainly resulted from collagen-forming amino acids, branched-chain amino acids, and matrikine-like peptides. Collectively, the residue of the perch extract can be upcycled via hydrolysis technique to produce not only bioactive sequences but also short chain peptides. Considering the therapeutic potential to promote wound healing, such by-products are of great value that may develop as dietary nutraceuticals.

A plethora of studies have demonstrated the bioactive properties of collagen peptides, including the promotion of wound healing and bone health. Research has demonstrated that these effects are attributable to their elevated biocompatibility and signaling capabilities. The present study investigated the effects of collagen peptides produced by enzymatic hydrolysis of perch scales on the induction of extracellular matrix formation and osteogenesis. The findings demonstrated that a combination of pre-heating and enzymatic hydrolysis resulted in the optimal peptide yield, with 94.9% of the peptides exhibiting a molecular weight below 1200 Daltons and containing elevated levels of hydroxyproline. The addition of perch scale collagen peptides to fibroblasts 890510-01F ATIT has been demonstrated to effectively induce the production of type I procollagen and fibronectin, a protein associated with the osteoblast phenotype and osteoblast differentiation. It is also worthy of note that experiments conducted using MC3T3-E1 osteoblasts indicate that collagen peptides significantly increased alkaline phosphatase activity by a factor of 1.46. This study demonstrates that collagen peptides derived from perch scales are enriched in bioactive peptides containing C-terminal tyrosine residues, including DYPRNHY and DPYNRHY. These findings provide a scientific basis for the future development of perch scale-derived collagen peptides as dietary supplements or functional food ingredients for promoting bone health.