期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 49, 期 6, 页码 2992-2997出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf001119u
关键词
ACE inhibitory peptide; bovine skin; three-step ultrafiltration membrane reactor; gelatin hydrolysate
Bovine skin gelatin was hydrolyzed with sequenial protease treatments in the order of Alcalase, Pronase E, and collagenase using a three-step ultrafiltration membrane reactor. The molecular weight distributions of the first, second, and third hydrolysates were 4.8-6.6, 3.4-6.6, and 0.9-1.9 kDa,,respectively. The angiotensin I converting enzyme (ACE) inhibitory activity of the third hydrolysate (IC50 = 0.689 mg/mL) was higher than that of the first and second hydrolysates. Two different peptides showing strong ACE inhibitory activity were isolated from the hydrolysate using consecutive chromatographic methods including gel filtration chromatography, ion-exchange chromatography, and reversed-phase high-performance liquid chromatography. The isolated peptides were composed of Gly-Pro-Leu and Gly-Pro-Val and showed IC50 values of 2.55 and 4.67 muM, respectively.
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