Journal
FOOD RESEARCH INTERNATIONAL
Volume 43, Issue 3, Pages 902-906Publisher
ELSEVIER
DOI: 10.1016/j.foodres.2009.12.012
Keywords
ACE inhibitory peptides; Processing; High pressure
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In this study, angiotensin I-converting enzyme (ACE) inhibitory peptides, which had previously been identified in an active gelfiltration fraction from tuna cooking juice, were examined for the stability of their inhibitory properties and composition changes during processing and in the presence of gastrointestinal proteases. Results indicated that ACE inhibitory peptides reserved almost the same composition before and after various temperatures (20-100 degrees C), levels of pressure (50-300 MPa) and pH (2-10) treatments. ACE inhibitory peptides retained 95-99% activity after simulated digestion. High Performance Liquid Chromatography (HPLC) chromatograph peptide mappings exhibited slight differences before and after temperature (100 degrees C) pressure (300 MPa) and pH (2, 10) treatments. Our results indicate that tuna cooking juice-derived ACE inhibitory peptides possess some degree resistance to the influence of temperature, pressure, pH treatments, and gastrointestinal proteases. (C) 2010 Elsevier Ltd. All rights reserved.
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