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Lizard fish (Saurida elongata) muscle protein was hydrolyzed using neutral protease to produce protein hydrolysate (LFPH), and the hydrolysis conditions were investigated using response-surface methodology. The optimum conditions for producing peptides with the highest angiotensin-I converting enzyme (ACE)-inhibitory activity were the following: enzyme-to-substrate ratio of 10,000 U/g, temperature of 48 °C, pH 7.0, and hydrolysis time of 2 h. Under these conditions, the ACE-inhibitory activity of LFPH and the degree of hydrolysis were 84% and 24%, respectively. A novel ACE-inhibitory peptide was isolated from LFPH using ultrafiltration, Sephadex G-15, and high-performance liquid chromatography. The amino acid sequence of the ACE-inhibitory peptide was identified as Ser-Pro-Arg-Cys-Arg (SPRCR), and its IC50 was 41 ± 1 µM.
| Authors: | Wu, Shanguang ; Sun, Jianhua ; Tong, Zhangfa ; Lan, Xiongdiao ; Zhao, Zhongxing ; Liao, Dankui | |
| Journal: | Marine Drugs | |
| Volume: | 10 | |
| Issue: | 5 | |
| Year: | 2012 | |
| Pages: | 1066 | |
| DOI: | 10.3390/md10051066 | |
| Publication date: | 18-05-2012 |
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