Antihypertensive Effect of Novel Angiotensin I Converting Enzyme Inhibitory Peptides Derived From Enzymatic Hydrolysis of Salmon Protamine

• Main Authors: Fikriyah Rasyad, 裴莉亞
• Other Authors: Tzou-Chi Huang
• Format: Others
• Language: en_US
• Published: 2015
• Online Access: http://ndltd.ncl.edu.tw/handle/02344255779417384070

碩士 === 國立屏東科技大學 === 生物科技系所 === 104 === Angiotensin I converting enzyme (ACE) inhibitory peptide is widely recognized as possible cures for hypertension. Bioactive peptides from natural sources, including marine fish, are more considered because it has no harm effects. The objective of this study is screeningthe presence of potential ACE inhibitory peptide from salmon protamine. ACE inhibitory peptide was obtained from salmon protamine after 16 hours of hydrolysis by various enzymes and followed by ultrafiltration on a 3 kDa molecular weight cut off (MWCO) membrane. Their sequences were analysed by Liquid Chromatography Tandem Mass Spectrometric (LC-MS/MS). ACE inhibitory activity was measured using Reverse Phase High Performa Liquid Chromatography (RP-HPLC).The most potential ACE inhibitory peptide was synthesized using a method of Solid Phase Peptide Synthesis. The results indicated that trypsin hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates with the IC50 value 135.96 µg/ml. LC-MS/MS analysis of tryptic protamine identified two major peaks with three peptide sequences, Ser-Ser-Arg-Pro-Ile-Arg (SR-6), Ser-Ser-Ser-Arg-Pro-Ile-Arg (SR-7), Pro-Arg-Arg-Ala-Ser-Arg (PR-6) which sourced from salmine of Chum Salmon (Oncorhynchus keta). Furthermore these two peakswere fractionated and the ACE inhibitory activity assay showed that fraction 2, belongs to SR-6 and SR-7 peptides, has the highest activity. IC50 value of peptide SR-7 was 94.98 ± 2.63 µM. Therefore, it can be concluded that salmon protamine has ACE inhibitory peptides and it may be beneficial for preventing hypertension and can be used as functional food ingredients.