Peptides with Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity from Defibrinated, Hydrolyzed Bovine Plasma

Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. Th...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2002-11, Vol.50 (24), p.6981-6988
Main Authors: Wanasundara, P. K. Janitha P. D, Ross, Andrew R. S, Amarowicz, Ryszard, Ambrose, Steve J, Pegg, Ronald B, Shand, Phyllis J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Angiotensin-Converting Enzyme Inhibitors - pharmacology
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Animals
Biological and medical sciences
Blood Proteins - metabolism
Blood Proteins - pharmacology
Cattle
Chromatography, Gel
Chromatography, High Pressure Liquid
Endopeptidases - metabolism
Fibrin
Food industries
Fundamental and applied biological sciences. Psychology
General pharmacology
Hippurates - analysis
Hippurates - metabolism
Medical sciences
Peptides - chemistry
Peptides - pharmacology
Peptidyl-Dipeptidase A - metabolism
Pharmacognosy. Homeopathy. Health food
Pharmacology. Drug treatments
Protein Hydrolysates - pharmacology
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Summary:Defibrinated bovine plasma (DBP) was treated with the microbial protease Flavourzyme to obtain protein hydrolysates with various degrees of hydrolysis (DH). The angiotensin I-converting enzyme (ACE) inhibiting activity of the hydrolyzed protein was assessed with hippuryl-His-Leu as the substrate. The amount of hippuric acid released, due to uninhibited ACE activity, was determined by high-performance liquid chromatography. ACE inhibiting (ACEI) activity was found to increase with increasing DH; the 43% DH hydrolysate exhibited the highest activity and had an IC50 of 1.08 mg/mL. Peptide fractions with high ACEI activity were isolated using size exclusion chromatography. The fraction that possessed the highest ACEI activity contained peptides with GYP, HL(I), HPY, HPGH, L(I)F, SPY, and YPH sequence motifs, as determined by reversed-phase liquid chromatography−tandem mass spectrometry using a novel immonium precursor-ion scanning technique. Some of these motifs correspond to sequences found in bovine serum albumin, a potential source of ACEI peptides in bovine plasma. Keywords: Angiotensin I-converting enzyme inhibitors; bioactive peptides; immonium precursor-ions; LC-MS; MALDI-TOF MS; plasma protein; peptide sequencing; protein hydrolysis
ISSN:0021-8561
1520-5118
DOI:10.1021/jf025592e