Assessment and Separation of Angiotensin I-Converting Enzyme Inhibitory Peptides in Chinese Soypaste
2015 ◽
Vol 11
(2)
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pp. 301-305
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Keyword(s):
Abstract A Chinese soypaste-derived fraction with potent angiotensin I-converting enzyme (ACE) inhibitory activity (IC50 = 25.9 μg/mL) was obtained by treating soypaste extract with 80% ethanol. The result of gradient reversed-phase high-performance liquid chromatography (RP-HPLC) suggested that bioactive peptides bearing some polarity groups made a substantial contribution to the ACE inhibitory activity. By mass spectrometric analysis, a component was separated as Glu-Ser-Gly-Asp which was then found to act in a dose-dependent manner against ACE activity as a non-competitive inhibitor, with an IC50 value of 2.297 mM.
2005 ◽
Vol 10
(3)
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pp. 239-243
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2014 ◽
Vol 23
(5)
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pp. 1661-1666
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2019 ◽
Vol 245
(3)
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pp. 535-544
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2002 ◽
Vol 50
(24)
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pp. 6981-6988
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2003 ◽
Vol 69
(9)
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pp. 5297-5305
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2011 ◽
Vol 5
(2)
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pp. 93
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