Abstract
Bioactive peptides from fish collagens with antioxidant properties have become a topic of great interest for health, food, and processing/preservation industries. To explore the high-value utilized way of scales produced during the fish processing, collagen hydrolysates of redlip croaker (Pseudosciaena polyactis) scales were prepared using six different proteases, and the hydrolysate (RSCH) prepared using neutrase showed the highest degree of hydrolysis (21.36 ± 1.18%) and 2,2-diphenyl-1-picrylhydrazyl (DPPH·) radical scavenging activity (30.97 ± 1.56%) among the six hydrolysates. Subsequently, six antioxidant peptides were purified from RSCH using membrane ultrafiltration and serial chromatography, and their amino acid sequences were identified as DGPEGR, GPEGPMGLE, EGPFGPEG, YGPDGPTG, GFIGPTE, and IGPLGA with molecular masses of 629.61, 885.95, 788.96, 762.75, 733.80, and 526.61 Da, respectively. Among six collagen peptides, GPEGPMGLE, EGPFGPEG, and GFIGPTE exhibited the strongest scavenging activities on DPPH· radical (EC50 0.59, 0.37, and 0.45 mg/mL), hydroxyl radical (EC50 0.45, 0.33, and 0.32 mg/mL), and superoxide anion radical (EC50 0.62, 0.47, and 0.74 mg/mL). GPEGPMGLE, EGPFGPEG, and GFIGPTE showed high inhibiting ability on lipid peroxidation in a linoleic acid model system and protective activities on oxidation-damaged DNA. More importantly, GPEGPMGLE, EGPFGPEG, and GFIGPTE could protect HepG2 cells from H2O2-induced oxidative damage through decreasing the levels of reactive oxygen species (ROS) and MDA and activating intracellular antioxidant enzymes of superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px). These results suggested that six collagen peptides (RCP1–RCP6), especially GPEGPMGLE, EGPFGPEG, and GFIGPTE, might serve as potential antioxidants applied in nutraceutical and pharmaceutical products.
Highlights
Collagen from mammal resources is widely employed in multifarious human applications, such as food, cosmetics, pharmaceutical/biomedical, and nutraceutical products [1,2,3]
Marine derived collagens with those undesirable characters are more hydrolyzed by proteases compared to mammal collagens and are suitable to be prepared for bioactive peptides [15]
ASC-RC were hydrolyzed by pepsin, neutrase, papain, trypsin, flavoenzyme, and alcalase, respectively, and the collagen hydrolysate prepared using neutrase, referred to RSCH, showed the highest degree of hydrolysis (DH, 21.36 ± 1.18%) among the six ASC-RC hydrolysates (Table 1)
Summary
Collagen from mammal resources is widely employed in multifarious human applications, such as food, cosmetics, pharmaceutical/biomedical, and nutraceutical products [1,2,3]. The application of mammal collagen and its derivatives from mammalian species arouses extensive attention and anxiety of consumers due to disease transmission-connected reasons, allergy problems, Mar. Drugs 2020, 18, 156; doi:10.3390/md18030156 www.mdpi.com/journal/marinedrugs. Marine derived collagens with those undesirable characters are more hydrolyzed by proteases compared to mammal collagens and are suitable to be prepared for bioactive peptides [15]. Bioactive peptides prepared using marine derived collagens and gelatins have attracted broad attention due to their various promising applications [16,17,18]
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