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. 2021 Aug 25;19(9):480. doi: 10.3390/md19090480

Table 3.

Antioxidant properties of fish waste protein hydrolysates.

Substrate Enzymes Bioactive Properties Studied and Peptide Sequence Reference
Striped catfish frame meat Papain
Bromelain
DPPH radical scavenging activity (90%), ferric reducing antioxidant power [92]
Goby muscle proteins Alcalase DPPH radical scavenging activity and reducing power [93]
Rastrelliger kanagurta backbone Pepsin
Papain
DPPH radical scavenging activity (36–46%) [94]
Salmon protein hydrolysate Pepsin DPPH radical scavenging activity (55%) [95]
Pink perch frame waste hydrolysate Papain
Bromelain
DPPH free radical scavenging activity (up to 90%), ferric reducing antioxidant power [42]
Salmon (Salmo salar) frame hydrolysates Alcalase
Papain
DPPH free radical scavenging ability, ABTS activity, ferric reducing antioxidant power (FRAP), metal chelating activity and oxygen radical antioxidant capacity (ORAC) [96]
Oreochromis niloticus Scale gelatin hydrolysate Alcalase
Pronase E
trypsin
pepsin
DPPH radical scavenging activity, hydroxyl radical scavenging activity and superoxide radical anion scavenging activity [97]
Black pomfret visceral protein hydrolysate Pepsin
trypsin
ά-chymotrypsin
DPPH radical scavenging activity, FRAP and metal chelating activity (Ala-Met-Thr-Gly-Leu-Glu-Ala) [98]
Alaska pollack frame protein hydrolysate Mackerel intestine crude enzyme Higher antioxidant Activity in terms of ferric thiocyanate for peptide fraction < 1 kDa
Peptide sequence: Leu-Pro-His-Ser-Gly-Tyr (627 Da)
[29]
Tuna backbone protein hydrolysate Alcalase, a-chymotrypsin, neutrase, papain,
pepsin and trypsin
Higher lipid peroxidation inhibition and DPPH free radical scavenging activity for peptide—VKAGFAWTANQQLS (1519 Da) [14]
Cod (Gadus macrocephalus) Alcalase, neutrase, papain, trypsin, pepsin, and α-chymotrypsin Electron spin resonance technique &
Thr-Gly-Gly-Gly-Asn-Val
[36]
Bluefin leatherjacket (Navodon septentrionalis) heads Papain DPPH radical scavenging activity, hydroxyl radicals and ABTS radicals and
Trp-Glu-Gly-Pro-Lys, Gly-Pro-Pro, and Gly-Val-Pro-Leu-Thr
[41]
Bluefin leatherjacket (Navodon septentrionalis) skin Trypsin, flavourzyme, neutrase, papain, alcalase, and pepsin, DPPH, hydroxyl radicals and oxygen scavenging assays
Gly-Ser-Gly-Gly-Leu, Gly-Pro-Gly-Gly-Phe-Ile, and Phe-Ile-Gly-Pro
[99]
Salmon by-product Alcalase, Flavourzyme, Neutrase, pepsin, Protamex, and trypsin DPPH and ABTS
Phe-Leu-Asn-Glu-Phe-Leu-His-Val
[39]
Horse mackerel (Magalaspis cordyla) viscera In vitro gastrointestinal digestion DPPH and hydroxyl radicals
Ala—Cys—Phe—Leu (518.5 Da)
[91]
Giant catfish (Pangasianodon gigas) skin Visceral alkaline-proteases from Giant catfish, commercial trypsin, Izyme AL® ABTS radical-scavenging, Ferric reducing antioxidant power (FRAP) and metal (ferrous) chelating ability [100]
Aisan seabass (Lates calcarifer) skin Protease from hepatopancreas of Pacific white shrimp, Alcalase DPPH and ABTS radical-scavenging activity, Ferric reducing antioxidant power, metal (ferrous) chelating activity, inhibition of lipid peroxidation [40]
Croaker (Otolithes ruber) skin Pepsin, trypsin, α-chymotrypsin Gly-Asn-Arg-Gly-Phe-Ala-Cys-Arg-His-Ala and
DPPH and hydroxyl radical-scavenging activity, ferric-reducing antioxidant power, metal (ferrous) chelating activity, inhibition of lipid peroxidation
[91]
Jumbo squid skin gelatin Enzymatic hydrolysis Good antioxidant activity for isolated peptide Phe-Asp-Ser-Gly-Pro Ala-Gly-Val-Leu [101]