ACE-inhibitory activity of tilapia protein hydrolysates

ACE-inhibitory activity of tilapia protein hydrolysates

Fish processing wastes can be used for preparing bioactive peptides with various functionalities. Our objective was to evaluate the in vitro angiotensin converting enzyme (ACE) inhibitory activity of tilapia protein hydrolysates and its corresponding fractionates. Tilapia protein was alkali-solubili...

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Veröffentlicht in:Food chemistry 2009-12, Vol.117 (4), p.582-588
Hauptverfasser: Raghavan, Sivakumar, Kristinsson, Hordur G.
Format: Artikel
Sprache:eng
Schlagworte:
Angiotensin converting enzyme inhibition
Biological and medical sciences
Cryotin
enzyme activity
enzyme inhibition
Flavourzyme
Food industries
food processing wastes
fractionation
Fundamental and applied biological sciences. Psychology
peptidyl-dipeptidase A
protein hydrolysates
separation
Tilapia
tilapia (common name)
Ultrafiltration
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Zusammenfassung:Fish processing wastes can be used for preparing bioactive peptides with various functionalities. Our objective was to evaluate the in vitro angiotensin converting enzyme (ACE) inhibitory activity of tilapia protein hydrolysates and its corresponding fractionates. Tilapia protein was alkali-solubilised at pH 11.0 and recovered at pH 5.5 to obtain a stable substrate. This substrate was hydrolysed using two enzymes, Cryotin-F or Flavourzyme, to 7.5% and 25% degree of hydrolysis (DH). The hydrolysates were ultra-filtered into three fractions: >30 kDa fraction, 10–30 kDa fraction, and
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2009.04.058