Preparation and identification of a novel antioxidative peptide from fermented protein hydrolysate of chicken (Gallus gallus domesticus) meat

Neelu Suresh, Babu and Suresh, P. V. and Tanaji Kudre, G. (2025) Preparation and identification of a novel antioxidative peptide from fermented protein hydrolysate of chicken (Gallus gallus domesticus) meat. Process Biochemistry, 151. pp. 167-176.

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Abstract

Present investigation deals with the preparation, purification, and identification of antioxidant peptides from fermented chicken (Gallus gallus domesticus) meat protein hydrolysate (CMPH). Antioxidant CMPH was pro­ duced by Pediococcus pentosaceus fermentation using 45 % chicken meat concentration, 2 % dextrose, and 48 h of fermentation time. Antioxidant peptides were separated from CMPH by employing ultrafiltration (3 kDa MWCO), Sephadex G-15 gel filtration chromatography, and RP-HPLC, respectively. Ultrafiltration (3 kDa MWCO) revealed that CMPH-UF-1 (MW < 3 kDa) exhibited significantly higher ferric-reducing antioxidant power (FRAP) (22.70 µM TE/mg), DPPH (30.77 µM TE/mg), and ABTS radical scavenging activity (39.41 µM TE/mg) and Fe2+chelating activity (21.45 µM EDTA/mg) than CMPH-UF-2 (p < 0.05). Six fractions of antioxidant peptides were separated from CMPH-UF-1 by Sephadex G-15 chromatography. Among these, CMPH-GF-5 peptide fraction unveiled significantly higher antioxidant activities with FRAP (38.21 µM TE/mg), DPPH radical scavenging activity (55.91 µM TE/mg), and ABTS radical scavenging activity (68.41 µM TE/mg) and Fe2+ chelating activity (36.96 µM EDTA/mg) (p < 0.05). Subsequent RP-HPLC purification of CMPH-GF-5 produced eleven fractions, among which CMPH-RPH-8 showed superior antioxidant activities with FRAP (65.06 µM TE/mg), DPPH radical scavenging activity (110.2 µM TE/mg), and ABTS radical scavenging activity (94.07 µM TE/mg) and Fe2+chelating activity (56.19 µM EDTA/mg). LC-MS/MS analysis identified a novel peptide in CMPH-RPH-8 (857.898 Da) with the sequence Leu-Gly-Gln-Glu-Ser-Leu-Ser-Pro-Asp, which has not been previously re­ported. Identified peptide was synthesized and verified the antioxidant activities. Therefore, the purified anti­oxidant peptide from CMPH is novel and can serve as a promising antioxidant in functional foods and nutraceutical products.

Item Type:	Article
Uncontrolled Keywords:	Chicken meat protein hydrolysate, Pediococcus pentosaceus fermentation, Antioxidant activity, Peptide purification, Peptide identification
Subjects:	500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 25 Peptide Chemistry 600 Technology > 08 Food technology > 28 Meat, Fish & Poultry
Divisions:	Meat Fish and Poultry Technology
Depositing User:	Somashekar K S
Date Deposited:	05 Mar 2025 10:06
Last Modified:	05 Mar 2025 10:06
URI:	http://ir.cftri.res.in/id/eprint/19177

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