Isolation, purification and identification of three novel antioxidative peptides from patin (Pangasius sutchi) myofibrillar protein hydrolysates

Leila Najafian, Abd. Salam Babji

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29 Citations (Scopus)

Abstract

Myofibrillar protein from patin was hydrolysed using papain, alcalase and flavourzyme with differing degrees of hydrolysis (DH) to obtain antioxidative peptides. The protein solubility and peptide content of the myofibrillar protein hydrolysates (MPHs) were observed. The antioxidant activity of the hydrolysates was evaluated. The results showed that the highest DH (89.17%) of MPH was produced by the 120-min papain treatment. When the DH of MPHs increased, protein solubility and peptide content increased. Papain-MPHs exhibited the highest antioxidant activity. The papain hydrolysate was purified using ion exchange chromatography, gel filtration chromatography and RP-HPLC. The potent fraction (MI 4) obtained from RP-HPLC had DPPH radical scavenging activity that was 2.97 times higher than MPH. Three antioxidative peptide sequences were identified as VPKNYFHDIV, LVMFLDNQHRVIRH, and FVNQPYLLYSVHMK according to HPLC and connected to the electrospray ionization-time-of-flight mass spectrometer (ESI-TOF MS/MS). The FVNQPYLLYSVHMK peptide exhibited the highest antioxidant activity. The presence of hydrophobic amino acids (Leu, Val and Phe), hydrophilic and basic amino acids, (His, Pro and Lys), and aromatic amino acids (Phe and Tyr) in the peptide sequences is believed to contribute to the high antioxidant activity of MPHs. These results suggest that MPHs from patin have potential as a natural antioxidants ingredient in foods.

Original languageEnglish
Pages (from-to)452-461
Number of pages10
JournalLWT - Food Science and Technology
Volume60
Issue number1
DOIs
Publication statusPublished - 1 Jan 2015

Fingerprint

Pangasianodon hypophthalmus
Protein Hydrolysates
myofibrillar proteins
protein hydrolysates
peptides
Papain
Peptides
papain
Antioxidants
antioxidant activity
Hydrolysis
High Pressure Liquid Chromatography
high performance liquid chromatography
protein solubility
hydrolysis
Solubility
hydrolysates
amino acids
Subtilisins
Basic Amino Acids

Keywords

  • Antioxidant peptides
  • Mass spectrometry
  • Myofibrillar protein hydrolysate
  • Patin (P.sutchi)
  • Purification

ASJC Scopus subject areas

  • Food Science

Cite this

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title = "Isolation, purification and identification of three novel antioxidative peptides from patin (Pangasius sutchi) myofibrillar protein hydrolysates",
abstract = "Myofibrillar protein from patin was hydrolysed using papain, alcalase and flavourzyme with differing degrees of hydrolysis (DH) to obtain antioxidative peptides. The protein solubility and peptide content of the myofibrillar protein hydrolysates (MPHs) were observed. The antioxidant activity of the hydrolysates was evaluated. The results showed that the highest DH (89.17{\%}) of MPH was produced by the 120-min papain treatment. When the DH of MPHs increased, protein solubility and peptide content increased. Papain-MPHs exhibited the highest antioxidant activity. The papain hydrolysate was purified using ion exchange chromatography, gel filtration chromatography and RP-HPLC. The potent fraction (MI 4) obtained from RP-HPLC had DPPH radical scavenging activity that was 2.97 times higher than MPH. Three antioxidative peptide sequences were identified as VPKNYFHDIV, LVMFLDNQHRVIRH, and FVNQPYLLYSVHMK according to HPLC and connected to the electrospray ionization-time-of-flight mass spectrometer (ESI-TOF MS/MS). The FVNQPYLLYSVHMK peptide exhibited the highest antioxidant activity. The presence of hydrophobic amino acids (Leu, Val and Phe), hydrophilic and basic amino acids, (His, Pro and Lys), and aromatic amino acids (Phe and Tyr) in the peptide sequences is believed to contribute to the high antioxidant activity of MPHs. These results suggest that MPHs from patin have potential as a natural antioxidants ingredient in foods.",
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AU - Babji, Abd. Salam

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N2 - Myofibrillar protein from patin was hydrolysed using papain, alcalase and flavourzyme with differing degrees of hydrolysis (DH) to obtain antioxidative peptides. The protein solubility and peptide content of the myofibrillar protein hydrolysates (MPHs) were observed. The antioxidant activity of the hydrolysates was evaluated. The results showed that the highest DH (89.17%) of MPH was produced by the 120-min papain treatment. When the DH of MPHs increased, protein solubility and peptide content increased. Papain-MPHs exhibited the highest antioxidant activity. The papain hydrolysate was purified using ion exchange chromatography, gel filtration chromatography and RP-HPLC. The potent fraction (MI 4) obtained from RP-HPLC had DPPH radical scavenging activity that was 2.97 times higher than MPH. Three antioxidative peptide sequences were identified as VPKNYFHDIV, LVMFLDNQHRVIRH, and FVNQPYLLYSVHMK according to HPLC and connected to the electrospray ionization-time-of-flight mass spectrometer (ESI-TOF MS/MS). The FVNQPYLLYSVHMK peptide exhibited the highest antioxidant activity. The presence of hydrophobic amino acids (Leu, Val and Phe), hydrophilic and basic amino acids, (His, Pro and Lys), and aromatic amino acids (Phe and Tyr) in the peptide sequences is believed to contribute to the high antioxidant activity of MPHs. These results suggest that MPHs from patin have potential as a natural antioxidants ingredient in foods.

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