Title of article :
Angiotensin I-converting enzyme inhibitory compounds in white and red wines
Author/Authors :
P.J. and Pozo-Bayَn، نويسنده , , M. ءngeles and Alcaيde، نويسنده , , Juan M. and Polo، نويسنده , , M. Carmen and Pueyo، نويسنده , , Encarnaciَn، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
5
From page :
43
To page :
47
Abstract :
The antihypertensive activity of 41 wines has been determined by measuring the inhibitory activity of angiotensin-converting enzyme. The activity determined ranges from 10.3% to 95.4%, with significantly higher mean values in red wines than in the other wines. The fraction molecular weight below 10,000 has been obtained in one white wine and in one red wine by ultrafiltration and then fractionating by low pressure liquid chromatography in a Sephadex LH-20 column. The amino acids of the peptides of 6 fractions that presented antihypertensive activity were determined. The amino acids Asx, Glx and Val, form part of 5 of the 6 fractions studied, and Thr and Ala part of 4 of these fractions. Valine, which is not a majority amino acid in wine peptides, is the majority amino acid in 5 of the 6 fractions with antihypertensive activity studied.
Keywords :
ACE-inhibitory compounds , Antihypertensive activity , amino acids , Wine peptides
Journal title :
Food Chemistry
Serial Year :
2007
Journal title :
Food Chemistry
Record number :
1953437
Link To Document :
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