Purification and identification of antioxidant peptides from gelatin hydrolysate of seabass skin

Abstract

Antioxidant peptides from gelatin hydrolysate of seabass (Lates calcarifer) skin prepared by Alcalase were isolated using a series of chromatographic techniques including Sephadex G‐25 column and reversed‐phase high performance liquid chromatography. Identification of the antioxidant peptides was carried out using UPLC–ESI‐MS/MS. Four potent antioxidant peptides with 5–12 amino acid residues were identified as Gly‐Leu‐Phe‐Gly‐Pro‐Arg (646.3671 Da), Gly‐Ala‐Thr‐Gly‐Pro‐Gln‐Gly‐Pro‐Leu‐Gly‐Pro‐Arg (1,107.5905 Da), Val‐Leu‐Gly‐Pro‐Phe (532.3130 Da), and Gln‐Leu‐Gly‐Pro‐Leu‐Gly‐Pro‐Val (780.4614 Da). The identified peptides were synthesized and analyzed for 2,2‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid radical scavenging activity. Gly‐Leu‐Phe‐Gly‐Pro‐Arg exhibited the highest antioxidant activity (81.41 mmol TE/µmol peptide) (P < .05). Therefore, peptides prepared from seabass skin could be employed as functional food ingredients. Practical applications Seabass skin, by‐product from fish processing industry, is a potential raw material for production of protein hydrolysates with bioactivities. Enzymatic cleavage of fish skin gelatin has been used to produce antioxidant peptides. In this study, the potent antioxidant peptides from seabass skin gelatin hydrolysate were purified and identified using a series of chromatographic techniques. Seabass skin gelatin hydrolysate could be used as potential functional food ingredient or nutraceutical with antioxidant activity.

Hydrolyzed collagen from porcine lipase‐defatted seabass skin: Antioxidant, fibroblast cell proliferation, and collagen production activities

“…For HC prepared by PPL pretreatment in conjunction with papain hydrolysis (Figure c), the 4,054 Da peptide peak was observed as the dominant group, followed by the 11,860 and 5,509 Da peaks. The results were consistent with a previous report that showed peptides from seabass skin gelatin (1,500–4,500 Da) exhibited antioxidant activity (Sae‐leaw et al, ). Similarly, low MW (156, 364, 1505 Da) antioxidant peptides were found to be present in the gelatin hydrolysate from seabass skin prepared using protease from Pacific white shrimp hepatopancreas (Senphan & Benjakul, ).…”

Antioxidant activities of hydrolysed collagen from salmon scale ossein prepared with the aid of ultrasound

“…Peptides from seabass skin gelatin hydrolysate with MW of 642 Da exerted the highest ABTS radical scavenging activity (Sae‐Leaw et al ., ). Peptides from blue shark skin gelatin hydrolysates with MWs ranging from 150 to 2000 Da possessed strong antioxidant activity (Weng et al ., ).…”

“…Hydrolysed collagen powders before and after gastrointestinal digestion were subjected to gel filtration chromatography as described by Sae‐Leaw et al . ().…”

“…Via enzymatic hydrolysis, those peptides with the unique Gly–Pro–Hyp sequence in their structures are liberated from mother collagen. However, bioactivities of peptides are associated with their amino acid compositions and sequences (Sae‐Leaw et al ., ).…”

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

“…Bioactive ingredients in food can improve health conditions and minimize the dependence on synthetic medicines (Rui, Boye, Simpson, & Prasher, ). In recent years, a number of studies on novel functional ingredients, such as hydrolyzed proteins and bioactive peptides from various food sources, have appeared (Ghassem, Babji, Said, Mahmoodani, & Arihara, ; Girgih, Udenigwe, & Aluko, ; Mane & Jamdar, ; Sae‐Leaw et al, ). Plant protein‐derived peptides have been less researched than those from animal sources, although plants are recognized as cheap sources of protein with many potential functional activities (Aluko, ; Cheng, Xiong, & Chen, ; Jahanbani et al, ; Megías et al, ; Valverde, Orona‐Tamayo, Nieto‐Rendón, & Paredes‐López, ; Vásquez‐Villanueva, Marina, & García, ).…”