Angiotensin I Converting Enzyme-Inhibitory Peptides from Wine

¹ The Institute of Enology and Viticulture, Yamanashi University, Kofu, Yamanashi 400-0005, Japan.

Six peptides that inhibit angiotensin I converting enzyme (ACE) were fractionated and purified from Muscat Bailey A red (Bailey x Muscat Hamburg) wine. Muscat Bailey A wine was concentrated to 1/2 of its original volume, then applied to a reverse phase open column. Peptides were eluted using a stepwise gradient of 0 to 90% ethanol. The fraction that eluted at 10% ethanol was the most inhibitory. Peptides in this fraction were separated into three active compound fractions (I, II, and III) by gel filtration on Toyopearl HW-40. These fractions were further separated by reverse-phase HPLC on a µBondasphere C₁₈ column, using a linear gradient of 0 to 50% acetonitrile into six peptides that inhibited ACE. The amino acid sequences and IC₅₀ values (concentration required for 50% ACE inhibition) of the purified peptides were LIPPGVPY (17.5 µM), YYAPFDGIL (83.0 µM), YYAPF (26.4 µM), SWSF (76.3 µM), WVPSVY (25.7 µM), and AWPF (18.3 µM).

Key words: angiotensin I converting enzyme, inhibitor, peptide, wine

Submitted on March 18, 1998
Revised on May 28, 1998