Isolation from alpha-zein of thermolysin peptides with angiotensin I-converting enzyme inhibitory activity.
Urea-denatured alpha-zein was almost completely hydrolyzed into small peptides by digestion with 1/100 (w/w) of thermolysin at 37 degrees C for 3h. The angiotensin I-converting enzyme (ACE) inhibitory activity (IC50) of the thermolysin digest of total alpha-zein was 24.5 micrograms/ml, and most of the peptide fractions from Z19 alpha-zein and total alpha-zein separated by reverse-phase HPLC had more or less ACE inhibitory activity. From these fractions, thirty-six peptides, including 5 dipeptides, 14 tripeptides, 9 tetrapeptides, 5 pentapeptides, and 3 hexapeptides, were purified and their amino acid sequences were determined.
Yano
S
S
Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Suzuki
K
K
Funatsu
G
G
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010455:Peptides / Q000302:isolation & purification*; D012995:Solubility; D013820:Thermolysin / Q000737:chemistry*; D014867:Water / Q000737:chemistry; D015028:Zein / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D014867:Water; D015028:Zein; D013820:Thermolysin