Preparation and antihypertensive activity of peptides from Porphyra yezoensis |
| |
Authors: | Wenjuan Qu Haile Ma Zhongli Pan Lin Luo Zhenbin Wang Ronghai He |
| |
Affiliation: | 1. School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, China;2. Jiangsu Provincial Research Center of Bio-process and Separation Engineering of Agri-products, Zhenjiang, Jiangsu 212013, China;3. USDA-ARS West Regional Research Center, Processed Foods Research Unit, 800 Buchanan Street, Albany, CA 94710, USA;4. Department of Biological and Agricultural Engineering, University of California, One Shields Avenue, Davis, CA 95616, USA |
| |
Abstract: | This research was to develop a antihypertensive peptide, an efficient angiotensin converting enzyme (ACE) inhibitor (ACEI), from Porphyra yezoensis. Seven commercial enzymes were screened and then enzymatic hydrolysis conditions were optimised. The results showed that alcalase was the most effective for hydrolysis and its optimum conditions for achieving the highest antihypertensive activity of peptide were 1.5% substrate, 5% alcalase, pH 9.0, and temperature of 50 °C at a hydrolysis time of 60 min. The antihypertensive peptide produced under the optimum conditions had a high ACE inhibition rate of 55.0% and a low IC50 value of 1.6 g/l and remained at high stability at temperatures of 4, 25, and 37 °C, pH values of 2.0 and 8.0, and after pepsin and trypsin treatments. Major proteins from P. yezoensis were glutelin, albumin, and gliadin. The albumin and glutelin had higher hydrolysis rates than the gliadin, but the IC50 value of glutelin was the lowest, which indicated that the antihypertensive peptide from glutelin was more functional. |
| |
Keywords: | Porphyra yezoensis Peptide Protein Enzymatic hydrolysis Central composite design Antihypertensive activity |
本文献已被 ScienceDirect 等数据库收录! |
|