Optimization of Hydrolysis Conditions for the Production of Angiotensin-I Converting Enzyme-Inhibitory Peptides and Isolation of a Novel Peptide from Lizard Fish Saurida elongata Muscle Protein HydrolysateReportar como inadecuado




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1

School of Chemistry and Chemical Engineering, Guangxi University, Nanning, Guangxi 530004, China

2

Department of Pharmacy, Liuzhou Medical College, Liuzhou, Guangxi 545006, China

3

Guangxi Key Laboratory of Petrochemical Resources Processing & Process Intensification Technology, Nanning, Guangxi 530004, China





*

Author to whom correspondence should be addressed.



Abstract 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. View Full-Text

Keywords: ACE-inhibitory peptide; lizard fish; enzymatic hydrolysis; response surface methodology; isolation ACE-inhibitory peptide; lizard fish; enzymatic hydrolysis; response surface methodology; isolation





Autor: Shanguang Wu 1,2, Jianhua Sun 1,3, Zhangfa Tong 1,3, Xiongdiao Lan 1, Zhongxing Zhao 1 and Dankui Liao 1,3,*

Fuente: http://mdpi.com/



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