Angiotensin I converting enzyme-inhibitory peptides from wine

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 mu Bondasphere C-18 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 mu M) YYAPFDGIL (83.0 mu M), YYAPF (26.4 mu M), SWSF (76.3 mu M), WVPSVY (25.7 mu M), and AWPF (18.3 mu M).