Abstract:
:A direct, extraction-free spectrophotometric assay was developed for determination of angiotensin I-converting enzyme activity (ACE) in the presence of ACE inhibitors using hippuryl-l-histidyl-l-leucine (HHL) as the ACE-specific substrate. This method relies on previously published spectrophotometric determination of hippuric acid (HA) content in the urine, the method of which was based on the specific colorimetric reaction of HA with benzene sulfonyl chloride (BSC) in the presence of quinoline. The proposed ACE inhibition assay was applied to the measurement of the ACE inhibitory activity of Captopril. IC(50) value of Captopril corresponded well with literature data. Furthermore, Alcalase hydrolysates of mung bean and rice protein isolates were assessed for ACE inhibitory activity by this method. These two hydrolysates showed high ACE inhibitory activity. This method proposed here was shown to be direct, sensitive, accurate, reproducible, and less expensive without separation of HA from ACE reaction mixture, and can be used for the screening of ACE inhibitory peptides derived from food proteins.
journal_name
J Pharm Biomed Analjournal_title
Journal of pharmaceutical and biomedical analysisauthors
Li GH,Liu H,Shi YH,Le GWdoi
10.1016/j.jpba.2004.11.004subject
Has Abstractpub_date
2005-02-23 00:00:00pages
219-24issue
2eissn
0731-7085issn
1873-264Xpii
S0731-7085(04)00574-6journal_volume
37pub_type
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journal_title:Journal of pharmaceutical and biomedical analysis
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