Purification and identification of novel antioxidant peptides from silkworm pupae (Bombyx mori) protein hydrolysate and molecular docking study

Effect of Silkworm Pupa Protein Hydrolysates on Proliferation of Gastric Cancer Cells In Vitro

“…Hydrophobic amino acids at the C-terminal and N-terminal also seemed to contribute to the antioxidant properties of active peptides. The SPPHs prepared by Khammuang, S et al [ 25 ] were proved to protect DNA from hydroxyl radical damage and the active polypeptides purified from their hydrolysate, AKPGVY and AAEYPA, had a good antioxidant effect. Xia, L et al [ 26 , 27 ] described a silkworm active peptide (amino acid sequence: MNFAKILSFVFALVALSMTSAAPEPRWKIFKKIKMGRNIRDGIVKAGPAIEVLGSAKAIGK), whose polar amino acid was positively charged and could form specific amphiphilic α-helices that interacted with the nonpolar lipid cell membrane and induced cytoskeleton destruction of esophageal cancer cells, and had no toxicity to some normal cells.…”

Bioactive Peptide Discovery from Edible Insects for Potential Applications in Human Health and Agriculture

“…In the past 10 years, enzymatic hydrolysis has been frequently adopted as a means of producing bioactive peptides from the proteins of edible insects. In such studies, silkworm pupae were relatively popular for the purpose of bioactive peptide discovery [ 29 , 30 , 31 , 32 , 33 ]. Figure 1 shows a general workflow employed by many studies in the discovery of bioactive peptides.…”

“…Among the numerous commercially available proteases, alcalase, flavourzyme, and Promod 278P were found to effectively generate functional hydrolysate/peptides from edible insects, leading to the discovery of antioxidant, anti-angiotensin-converting enzyme (ACE), anti-dipeptidyl peptidase-IV (DPP-IV), anti-obesity and hepatoprotective peptides ( Table 1 ). However, alcalase received the most attention as it produced more potent peptides [ 29 , 30 , 34 ]. This could be because alcalase exhibits both endo- and exo-protease activities, which allows a broad specificity in hydrolysis sites [ 29 ], thus providing relatively extensive hydrolysis of the insect proteins.…”

“…Ultrafiltration was often the first step in peptide purification, probably because of its simplicity and cost-effectiveness. The ultrafiltration membranes used mostly had molecular weight cut-offs (MWCO) of 1, 3, 5, and 10 kDa [ 30 , 31 , 33 , 34 , 35 , 36 , 37 , 38 ]. The peptide fraction with the lowest molecular weight very often showed the highest bioactivity, and thus, was chosen to proceed to the next purification step.…”

“…Most studies presented in Table 1 purified the bioactive peptides of interest by using the reversed-phase high-performance liquid chromatography (RP-HPLC) in the last step prior to amino acid sequencing. Hydrophobic amino acids contribute to the activities of anti-ACE, anti-DPP-IV, and antioxidant peptides [ 30 , 31 , 32 , 33 , 35 , 38 , 39 ]. Thus, this may rationalize the use of RP-HPLC columns in isolating the aforementioned bioactive peptides from insect protein hydrolysates.…”