In vitro analysis of antioxidant peptides from an enzymatically hydrolysed Channa punctata protein isolate
Madhushrita Das
Department of Chemical Technology, University of Calcutta, Kolkata, India
Search for more papers by this authorCorresponding Author
Mahua Ghosh
Department of Chemical Technology, University of Calcutta, Kolkata, India
Correspondence
Mahua Ghosh, Department of Chemical Technology, University of Calcutta, 92, A. P. C Road, Kolkata-700009, West Bengal, India.
Email: [email protected]
Search for more papers by this authorMadhushrita Das
Department of Chemical Technology, University of Calcutta, Kolkata, India
Search for more papers by this authorCorresponding Author
Mahua Ghosh
Department of Chemical Technology, University of Calcutta, Kolkata, India
Correspondence
Mahua Ghosh, Department of Chemical Technology, University of Calcutta, 92, A. P. C Road, Kolkata-700009, West Bengal, India.
Email: [email protected]
Search for more papers by this authorAbstract
Channa punctata, a freshwater fish consists of a good amount of protein (64.42 ± 0.51%) with essential amino acids. The degree of hydrolysis was maximum at 240 min with 82.72 ± 0.89% and 21.37 ± 1.21% of hydrolysis in the case of Alcalase 2.4 L (AlcHyd240) and pepsin (PepHyd240). Low molecular weight bands (<10 kDa) were more prominent in AlcHyd240. Hydrolysate shows improved functional properties in comparison with isolate. <3 kDa ultrafiltrate shows enhanced antioxidative efficacy than the hydrolysate and isolate. The fractions were analysed by MALDI-TOF MS/MS and two peptides PLRVGN and PLPNSK with the highest score of 70.4 and 56.5, respectively and hydrophobicity of 50% were selected for in vitro study. Molecular docking studies revealed that peptides interacted with the radicals by H-bond. The presence of proline, leucine, valine, glycine, arginine, serine, and lysine induces antioxidant activity. Thus, this study suggested the peptides identified from Channa punctata can be used as a nutraceutical with potent antioxidant activity.
Novelty impact statement
- A potent antioxidant Channa punctata protein hydrolysates were generated by enzymatic hydrolysis and were purified by ultrafiltration.
- Amino acid sequences PLRVGN and PLPNSK were identified by using MALDI-TOF MS/MS. Docking study revealed H-bond interactions between the peptides and the free radical.
- According to the structure–activity relationship study, the presence of hydrophobic amino acid residues, glycine, and serine influences the antioxidant potential.
CONFLICTS OF INTEREST
There are no conflicts of interest to declare.
Open Research
DATA AVAILABILITY STATEMENT
The data that support the findings of this study are available from the corresponding author upon reasonable request.
Supporting Information
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