Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Assessment of the Inhibitory Activity of Peptide Extracts from Hanwoo Musculus Longissimus on Angiotensin I-Converting Enzyme

  • Seol, Kuk-Hwan (National Institute of Animal Science, Rural Development Administration) ;
  • Song, Ji-Hye (CJ Cheiljedang Corporation Foods R&D Nutraceuticals & Functional Foods Center) ;
  • Prayad, Thirawong (Department of Animal and Food Biotechnology, Research Institute for Agriculture and Life Science, Seoul National University) ;
  • Kim, Hyoun-Wook (National Institute of Animal Science, Rural Development Administration) ;
  • Jang, Ae-Ra (National Institute of Animal Science, Rural Development Administration) ;
  • Ham, Jun-Sang (National Institute of Animal Science, Rural Development Administration) ;
  • Oh, Mi-Hwa (National Institute of Animal Science, Rural Development Administration) ;
  • Kim, Dong-Hun (National Institute of Animal Science, Rural Development Administration) ;
  • Lee, Moo-Ha (Department of Animal and Food Biotechnology, Research Institute for Agriculture and Life Science, Seoul National University)
  • Received : 2010.11.29
  • Accepted : 2011.09.16
  • Published : 2011.10.31
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Abstract

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

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References

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