Angiotensin i-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats
In: Food chemistry, Jg. 94 (2005), Heft 1, S. 26-32
academicJournal
- print, 33 ref
Zugriff:
In order to utilize yellowfin sole (Limanda aspera) frame protein, which is normally discarded as industrial waste in the process of fish manufacture, yellowfin sole frame protein was hydrolysed by α-chymotrypsin. Yellowfin sole frame protein hydrolysates (YFPHs) were fractionated into three ranges of molecular weight (YFPH-I, 30-10 kDa; YFPH-II, 10-5 kDa; YFPH-III, below 5 kDa) using an ultrafiltration (UF) membrane bioreactor system. Angiotensin I-converting enzyme (ACE) inhibitory activity was detected on YFPH-III, and the ACE inhibitory peptide (YFP) was purified from YFPH-III using consecutive chromatographic techniques. The YFP with a molecular mass of 1.3 kDa consisted of 11 amino acids, Met-Ile-Phe-Pro-Gly-Ala-Gly-Gly-Pro-Glu-Leu, and its IC50 value was 28.7 μg/ml. Lineweaver-Burk plots suggest that YFP acts as a non-competitive inhibitor to inhibit ACE. Antihypertensive effects of YFP on spontaneously hypertensive rats (SHR) following oral administration was determined as the blood pressure significantly decreased after peptide ingestion.
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Angiotensin i-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats
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Autor/in / Beteiligte Person: | JUNG, Won-Kyo ; MENDIS, Eresha ; JE, Jae-Young ; PARK, Pyo-Jam ; BYENG WHA, SON ; HYOUNG CHIN, KIM ; YANG KYU, CHOI ; KIM, Se-Kwon |
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Zeitschrift: | Food chemistry, Jg. 94 (2005), Heft 1, S. 26-32 |
Veröffentlichung: | Oxford: Elsevier, 2005 |
Medientyp: | academicJournal |
Umfang: | print, 33 ref |
ISSN: | 0308-8146 (print) |
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