International Journal of Peptide Research and Therapeutics

, Volume 20, Issue 2, pp 209-219

First online:

Antioxidant Activity of Purified Protein Hydrolysates from Northern Whiting Fish (Sillago sihama) Muscle

  • K. VenkatesanAffiliated withDepartment of Biotechnology, School of Bioengineering, SRM University
  • , R. A. NazeerAffiliated withDepartment of Biotechnology, School of Bioengineering, SRM University Email author 

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In the present study, northern whiting fish (Sillago sihama) muscle was hydrolyzed with gastrointestinal enzymes (pepsin, trypsin and α-chymotrypsin) separately and the resulted protein hydrolysates were tested for antioxidant activities using DPPH radical scavenging activity and reducing power assays. The protein hydrolysate obtained from trypsin exhibited highest antioxidant activity. Further, it was fractionated by consecutive chromatography using anion exchange and gel filtration chromatography; the separated fractions were collected and evaluated for antioxidant activity. The results showed that fraction 2 exhibited high chelating activity (73.15 % at 0.5 mg/mL) and best radical scavenging activity for DPPH radical (55.16 % at 0.5 mg/mL), ABTS radical (57.98 % at 50 μg/mL), superoxide radical (39.55 % at 200 μg/mL) and hydroxyl radical (51.33 % at 100 μg/mL). In addition, the active fraction showed strong antioxidant activity in the inhibition of linoleic acid autooxidation (60 % at 0.5 mg/mL) and also it exhibited significant protective effect on DNA damage caused by hydroxyl radicals. The size of the active fraction was found to be <360.2 Da using mass spectroscopy. These results demonstrate that muscle protein hydrolysate from northern whiting fish could be a best alternative to produce natural antioxidant peptides.


Antioxidant peptides Muscle protein hydrolysates Consecutive chromatography Mass spectrometer