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

IF 3.7 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Neelu Suresh Babu , P.V. Suresh , Tanaji G. Kudre
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引用次数: 0

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 produced 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.
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来源期刊
Process Biochemistry
Process Biochemistry 生物-工程:化工
CiteScore
8.30
自引率
4.50%
发文量
374
审稿时长
53 days
期刊介绍: Process Biochemistry is an application-orientated research journal devoted to reporting advances with originality and novelty, in the science and technology of the processes involving bioactive molecules and living organisms. These processes concern the production of useful metabolites or materials, or the removal of toxic compounds using tools and methods of current biology and engineering. Its main areas of interest include novel bioprocesses and enabling technologies (such as nanobiotechnology, tissue engineering, directed evolution, metabolic engineering, systems biology, and synthetic biology) applicable in food (nutraceutical), healthcare (medical, pharmaceutical, cosmetic), energy (biofuels), environmental, and biorefinery industries and their underlying biological and engineering principles.
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