Antioxidant and anti-freezing peptides from salmon collagen hydrolysate prepared by bacterial extracellular protease

Wü, Ray; Wu, Chen; Liu, Dan; Yang, Xinghao; Huang, Jiafeng; Zhang, Jiang; Liao, Binqiang; He, Hui

doi:10.1016/j.foodchem.2017.12.035

Cited by 122 publications

(79 citation statements)

References 28 publications

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“…[Ca 2+ ] did not have an obvious influence on the radical scavenging rate of these two collagen peptides, which corresponded with the reducing power trend. The antioxidants of GBB‐10SP and TYPE‐S were more significant than some special collagen and its peptide (Wen et al, ; Wu et al, ).…”

Section: Resultsmentioning

confidence: 99%

Effects of ion concentrations on the hydroxyl radical scavenging rate and reducing power of fish collagen peptides

Shen

Liu

et al. 2019

J Food Biochem

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Empirical evidence proves that the antioxidant property plays a main role in the biological activities of biomaterials, which is influenced by several factors. In order to explore in‐depth, the influence of ionic systems on the antioxidant activity of collagen peptides was studied. Type‐I‐collagen peptides (GBB‐10SP and TYPE‐S) contained a high amount of hydrophobic amino acids and possessed good antioxidant activity at high concentrations in water. On the other hand, increasing [H+] and [Na+] concentrations (0.1 M to 0.5 M) decreased the reducing power of GBB‐10SP and TYPE‐S; however, [Ca2+] had no effect on the reducing power. Interestingly, the hydroxyl radical scavenging rate of these two peptides was increased by [Na+], decreased by [H+], and [Ca2+] had no effect. In general, TYPE‐S showed better antioxidant properties than GBB‐10SP. Overall, the above results confirmed that the antioxidant capacity of collagen peptides was affected by [H+] and [Na+] and not by [Ca2+]. Practical applications The present study mainly deals with the influence of ions on the antioxidant properties of collagen peptides. Recently, fish collagen peptides have been widely used as food supplements to cure several disorders and maintain normal physiological health in humans. It is noted that the use of collagen from fish processing wastes has brought several potential benefits including low value‐added products, preventing environmental pollution, and disease transmission by mammalian‐based collagen. But the biological activity of this peptide varied based on the preparation and its biochemical compositions. Here, we are reporting how to improve the biological activity of collagen, and also the factors affecting the antioxidant properties in order to avoid the down‐regulating mechanism. This study concluded that the [H+] and [Na+] influenced the antioxidant properties of collagen peptides, but [Ca2+] had not effect on the antioxidant properties.

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Section: Resultsmentioning

confidence: 99%

Effects of ion concentrations on the hydroxyl radical scavenging rate and reducing power of fish collagen peptides

Shen

Liu

et al. 2019

J Food Biochem

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“…Zheng et al reported that hydrophobic amino acid residues (Leu and Ile) in AEDKKLIQ played an important role on the hydrophobic targets [55]. Met residue acted as a reactive site in the PMRGGGGYHY, WMFDW, WMGPY, and EMGPA through formatting a sulfoxide structure to scavenge free radicals [18,56]. Pro residue can help antioxidant peptides, such as LDEPDPL, WMGPY and EMGPA, scavenge ROS because of the pyrrolidine ring [18,57].…”

Section: Structure-activity Relationship Of Mmp-4 Mmp-7 and Mmp-12mentioning

confidence: 99%

Antioxidant Peptides from the Protein Hydrolysate of Monkfish (Lophius litulon) Muscle: Purification, Identification, and Cytoprotective Function on HepG2 Cells Damage by H2O2

Wang

Zhao

et al. 2020

Marine Drugs

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In the work, defatted muscle proteins of monkfish (Lophius litulon) were separately hydrolyzed by pepsin, trypsin, and in vitro gastrointestinal (GI) digestion methods, and antioxidant peptides were isolated from proteins hydrolysate of monkfish muscle using ultrafiltration and chromatography processes. The antioxidant activities of isolated peptides were evaluated using radical scavenging and lipid peroxidation assays and H2O2-induced model of HepG2 cells. In which, the cell viability, reactive oxygen species (ROS) content, and antioxidant enzymes and malondialdehyde (MDA) levels were measured for evaluating the protective extent on HepG2 cells damaged by H2O2. The results indicated that the hydrolysate (MPTH) prepared using in vitro GI digestion method showed the highest degree of hydrolysis (27.24 ± 1.57%) and scavenging activity on a 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (44.54 ± 3.12%) and hydroxyl radical (41.32 ± 2.73%) at the concentration of 5 mg protein/mL among the three hydrolysates. Subsequently, thirteen antioxidant peptides (MMP-1 to MMP-13) were isolated from MPTH. According to their DPPH radical and hydroxyl radical scavenging activity, three peptides with the highest antioxidant activity were selected and identified as EDIVCW (MMP-4), MEPVW (MMP-7), and YWDAW (MMP-12) with molecular weights of 763.82, 660.75, and 739.75 Da, respectively. EDIVCW, MEPVW, and YWDAW showed high scavenging activities on DPPH radical (EC50 0.39, 0.62, and 0.51 mg/mL, respectively), hydroxyl radical (EC50 0.61, 0.38, and 0.32 mg/mL, respectively), and superoxide anion radical (EC50 0.76, 0.94, 0.48 mg/mL, respectively). EDIVCW and YWDAW showed equivalent inhibiting ability on lipid peroxidation with glutathione in the linoleic acid model system. Moreover, EDIVCW, MEPVW, and YWDAW had no cytotoxicity to HepG2 cells at the concentration of 100.0 µM and could concentration-dependently 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 present results indicated that the protein hydrolysate and isolated antioxidant peptides from monkfish muscle, especially YWDAW could serve as powerful antioxidants applied in the treatment of some liver diseases and healthcare products associated with oxidative stress.

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“…In general, the numerical response of DPPH method, Crocin protocol was never employed to analyze salmonid samples, was not sufficiently attractive when are compared with samples of Alcalase hydrolysates from trout roe [25] and for soluble proteins obtained by chemical solubilization of a mixture of RT by-products [33]. However, enzymatic hydrolysates from pectoral fin and collagen skin of salmon showed similar % of DPPH than those listed in Table 6 [34,35]. Based on data from FPHs of other marine wastes, our DPPH activities were greater than hydrolysates of hake [36] and lower than samples of cuttlefish, herring, or croaker [37][38][39].…”

Section: In Vitro Bioactivities Of Hydrolysates From Salmonids By-promentioning

confidence: 99%

Valorization of Aquaculture By-Products of Salmonids to Produce Enzymatic Hydrolysates: Process Optimization, Chemical Characterization and Evaluation of Bioactives

et al. 2019

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In the present manuscript, various by-products (heads, trimmings, and frames) generated from salmonids (rainbow trout and salmon) processing were evaluated as substrates for the production of fish protein hydrolysates (FPHs), potentially adequate as protein ingredients of aquaculture feeds. Initially, enzymatic conditions of hydrolysis were optimized using second order rotatable designs and multivariable statistical analysis. The optimal conditions for the Alcalase hydrolysis of heads were 0.1% (v/w) of enzyme concentration, pH 8.27, 56.2 • C, ratio (Solid:Liquid = 1:1), 3 h of hydrolysis, and agitation of 200 rpm for rainbow trout and 0.2% (v/w) of enzyme, pH 8.98, 64.2 • C, 200 rpm, 3 h of hydrolysis, and S:L = 1:1 for salmon. These conditions obtained at 100 mL-reactor scale were then validated at 5L-reactor scale. The hydrolytic capacity of Alcalase and the protein quality of FPHs were excellent in terms of digestion of wastes (V dig > 84%), high degrees of hydrolysis (H m > 30%), high concentration of soluble protein (Prs > 48 g/L), good balance of amino acids, and almost full in vitro digestibility (Dig > 93%). Fish oils were recovered from wastes jointly with FPHs and bioactive properties of hydrolysates (antioxidant and antihypertensive) were also determined. The salmon FPHs from trimmings + frames (TF) showed the higher protein content in comparison to the rest of FPHs from salmonids. Average molecular weights of salmonid-FPHs ranged from 1.4 to 2.0 kDa and the peptide sizes distribution indicated that hydrolysates of rainbow trout heads and salmon TF led to the highest percentages of small peptides (0-500 Da). 676 2 of 15 and volume terms in the European fish farming system. More than 1.78 MTm of both were produced in 2016 generating more than € 15 billion [1]. Although in southern Europe the most common way to market salmonids is as complete individuals, in the rest of the continent the tendency is to market them in the form of fillets (fresh, frozen, cured, etc.) or other presentations that require deheading, gutting, and filleting steps. Thus, huge amounts of by-products (about 35-45% of the total weight of salmonids) are generated in processing plants, mainly heads, trimmings, viscera, and frames that have to be managed efficiently to reduce environmental health problems and to improve the sustainability of such farming productions [2,3].The most habitual utilization of salmonid wastes is based on the development of acid silage [3], fertilizers, or the joint production of fishmeal and oils [4,5]. In the first case, the silage is a low-added value product with limited applications [1]. In the last one, oil and fishmeal are not very sustainable productions when the fishmeal equipments are far from fishing ports or aquaculture plants and close to villages and cities due to the environmental impact (odors, air pollution, water consumption, etc.) that this production generates. This process leads to the coagulation of the protein and its separation from the oil but the level of valorization achieved by b...

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Antioxidant and anti-freezing peptides from salmon collagen hydrolysate prepared by bacterial extracellular protease

Cited by 122 publications

References 28 publications

Effects of ion concentrations on the hydroxyl radical scavenging rate and reducing power of fish collagen peptides

Effects of ion concentrations on the hydroxyl radical scavenging rate and reducing power of fish collagen peptides

Antioxidant Peptides from the Protein Hydrolysate of Monkfish (Lophius litulon) Muscle: Purification, Identification, and Cytoprotective Function on HepG2 Cells Damage by H2O2

Valorization of Aquaculture By-Products of Salmonids to Produce Enzymatic Hydrolysates: Process Optimization, Chemical Characterization and Evaluation of Bioactives

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