Journal
MEAT SCIENCE
Volume 90, Issue 1, Pages 226-235Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2011.07.008
Keywords
Antioxidant peptides; Bovine meat; Papain; Hydrolysis; Brisket muscle; ACE-I inhibitory peptides
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Funding
- Teagasc Walsh Fellowship
- Department of Agriculture, Fisheries and Food
- Food Institutional Research Measure (FIRM) [06/RD/TAFR/C472]
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The main objective was to investigate the angiotensin-l-converting enzyme (ACE-I) inhibitory and antioxidant activities of sarcoplasmic proteins isolated from the brisket muscle (Pectoralis profundus) of 3 (Bos taurus) cattle and hydrolysed with papain for 24 h at 37 degrees C. Sarcoplasmic protein hydrolysates were ultra-filtered using molecular weight cut off (MWCO) membranes and 10-kDa and 3-kDa filtrates were obtained. The total sarcoplasmic protein extracts and the 3-kDa filtrates were tested for angiotensin I-converting enzyme inhibitory (ACE-I) activities. The total hydrolysates, 10-kDa and 3-kDa filtrates were also tested for their associated antioxidant activities using the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity assay, the ferric ion reducing antioxidant power (FRAP) assay and the Fe2+ metal chelating ability assay. The peptidic content of the total hydrolysates, the 10-kDa and the 3-kDa filtrates were analysed using an ORBITRAP mass spectrometer, and mass spectral data obtained were analysed using TurboSEQUEST. Eleven peptides were characterised from the total hydrolysates, fifteen from the 10-kDa filtrate fractions, whilst nine peptides were characterised from the 3-kDa filtrate fractions. Similarities between the amino acid sequences of the peptides identified in this study and previously identified antioxidant and ACE-I inhibitory peptides detailed in the BIOPEP database were outlined. (C) 2011 Elsevier Ltd. All rights reserved.
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