Assessment of the spectrophotometric method for determination of angiotensin-converting-enzyme activity: influence of the inhibition type

J Agric Food Chem. 2003 Jul 16;51(15):4175-9. doi: 10.1021/jf034148o.

Abstract

A set of in vitro assay conditions were selected for the determination of ACE-inhibitory activity, and the need was demonstrated to standardize this assay so that the results obtained by different authors may be comparable. The conditions selected were as follows: 10 mM HHL concentration in 0.2 M potassium phosphate buffer and 0.3 M NaCl and 26 mU of ACE/mL as reaction medium; incubation time, 80 min at 37 degrees C. The method was applied to the study of ACE-inhibitory activity of dairy product and wine samples. Of the samples assayed, it was infant formulae whey that produces the greatest ACE inhibition. Red wine also presents a high inhibition percentage. This latter sample has an important matrix effect that must be corrected in the calculation. ACE-inhibition type was also studied, using a yogurt whey and a Captropil solution as substrates. The whey produced noncompetitive inhibition and the Captropil competitive inhibition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / analysis*
  • Animals
  • Captopril / pharmacology
  • Humans
  • Infant
  • Infant Food / analysis
  • Lung / enzymology
  • Milk Proteins / analysis
  • Oligopeptides / pharmacology
  • Peptidyl-Dipeptidase A / metabolism*
  • Rabbits
  • Spectrophotometry / methods*
  • Whey Proteins
  • Wine / analysis
  • Yogurt / analysis

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Milk Proteins
  • Oligopeptides
  • Whey Proteins
  • hippuryl-histidyl-leucine
  • Captopril
  • Peptidyl-Dipeptidase A