Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Bonito Bowels Autolysate (original) (raw)
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Current Pharmaceutical Design, 2009
The existence of endogenous bioactive protein or peptide with angiotensin-converting enzyme (ACE) inhibitory activity in snakehead fish fillet is promising to be investigated. The purposes of this research were to extract ACE inhibitory endogenous protein or peptide from snakehead fish fillet and to fractionate the active compounds using ultrafiltration. The extraction employed two solvents, i.e. aquadest and 50% ethanol. Fractionation was conducted using ultrafiltration membranes of 10,000; 5,000 and 3,000 Molecular W eight Cut Off (MW CO) to separate the protein or peptide into the sizes of >10 kDa, 5-10 kDa, 3-5 kDa and <3 kDa. The parameters observed were protein and peptide content, ACE inhibitory activity (in vitro) and also protein and peptide profiles. The result revealed that the snakehead fish fillet contained ACE inhibitory endogenous bioactive protein or peptide. The 50% ethanol was more effective in extracting peptide of <10 kDa than the aquadest. Yet, the aquadest was better in extracting higher molecular weight protein of >10 kDa than the 50% ethanol. The fraction of <3 kDa by aquadest had the highest ACE inhibitor activity per g protein (7.85% inhibition of ACE per g protein). Thus, the fraction of <3 kDa aquadest is the most promising option for further research and development of natural anti-hypertension compound. From the result, snakehead fish fillet was potential to be utilized as a functional food as well as functional ingredient to fight hypertension.
Journal of agricultural and food …, 2007
To investigate biomedical and nutraceutical benefits of bullfrog (Rana catesbeiana Shaw) muscle protein, we examined an angiotensin Iconverting enzyme (ACE I) inhibitory activity of various enzymatic hydrolystes of R. catesbeiana muscle protein in the present study. Among the enzymatic hydrolysates prepared using various commercial enzymes such as Alcalase, neutrase, pepsin, papain, a-chymotrypsin, and trypsin, Alcalase-proteolytic hydrolysates showed the highest ACE I inhibitory activity. During consecutive purification using a Hiprep 16/10 DEAE FF anion exchange and an octadecylsilane (ODS) C18 reversed phase liquid chromatographic techniques, a potent ACE I inhibitory peptide composed of 12 amino acids, Gly-Ala-Ala-Glu-Leu-Pro-Cys-Ser-Ala-Asp-Trp-Trp (M w : 1.3 kDa) was isolated from R. catesbeiana muscle hydrolysates degraded by Alcalase. The purified peptide from R. catesbeiana muscle (RCMP-alca) has IC 50 value of 0.95 mM, and Lineweaver-Burk plots suggest that RCMP-alca play act as a non-competitive inhibitor against ACE I. Antihypertensive effect in spontaneously hypertensive rats (SHR) also revealed that oral administration of RCMP-alca can decrease systolic blood pressure significantly (P < 0.05). In addition, MTT assay showed no cytotoxicity on human embryonic lung fibroblasts cell line . The result of this study suggests that the ACE inhibitory peptide derived from R. catesbeiana muscle (RCMP-alca) could be potential candidates to develop nutraceuticals and pharmaceuticals. #
Nutrition Research, 2004
Angiotensin I-converting enzyme (ACE) catalyzes the conversion of angiotensin I to vasoconstrictor angiotensin II, and also inactivates the antihypertensive vasodilator bradykinin. Inhibition of ACE mainly results in an overall antihypertensive effect. Peptides derived from food proteins can have ACE inhibiting properties. This article reviews the ACE inhibitory peptides derived from different food proteins. Some of the ACE inhibitory peptides exhibit significant antihypertensive effects. However, the inhibitory potencies of these peptides on ACE activity do not always correlate with their antihypertensive activities. Some peptides with high inhibitory activity on this enzyme in vitro have no blood pressure lowering effects, whereas some peptides with low inhibitory activity on this enzyme in vitro have such effects. The possible mechanisms for this conflicting phenomenon between inhibitory activity and antihypertensive effect, the structure-activity relationships, and the potential use prospect of these peptides in the development of a novel functional food for preventing hypertension as well as therapeutic purposes, are also discussed.
Malaysian Applied Biology
Blood cockle (Anadara granosa) is the most abundant and available bivalves in Malaysia. Blood cockles meat has high protein content and has potential to generate bioactive peptides. To date, no study has been reported on purification and identification of angiotensin I converting enzyme (ACE) inhibitory peptides from blood cockle meat. Thus, the objectives of this study were to purify and characterize ACE inhibitory peptide from blood cockle meat hydrolysate. ACE inhibitory peptides from blood cockle meat hydrolysate (CMH) were prepared by enzymatic protein hydrolysis using Protamex®. Crude CMH was characterized for its stability against gastrointestinal proteases, at varying pH (2–11) and temperature (4–90°C). Next, crude CMH was purified by ultrafiltration, ion exchange chromatography and reverse-phase chromatography and its amino acid sequence was identified. It was found that crude CMH was highly stable at low pH and temperature, and was resistant to gastrointestinal proteases (...
Angiotensin I Converting Enzyme Inhibitory Peptides from Fish By-products
CRC Press eBooks, 2013
Three peptides which inhibit angiotensin I-converting enzyme were isolated from maitake (Gnfola frondosa) water extract digested by pepsin. Among them, Lys-Tyr-Thr-Phe-Ala-Val-Thr-Thr-Val-Lys-Thr-Trp-Val had the strongest angiotensin I-converting enzyme inhibitory activity with an IC50 value of 2.6 uM, and the others Gly-Pro-Ser-Gly-Pro-Ser-Gly, and Tyr-Pro-Ser also showed inhibitory activity with IC50 values of 2160 and 570 uM, respectively!
Food Chemistry, 2013
This study aimed to identify novel ACE inhibitory peptides from the muscle of cuttlefish. Proteins were hydrolyzed and the hydrolysates were then subjected to various types of chromatography to isolate the active peptides. Nine ACE inhibitory peptides were isolated and their molecular masses and amino acid sequences were determined using ESI-MS and ESI-MS/MS, respectively. The structures of the most potent peptides were identified as Val-Glu-Leu-Tyr-Pro, Ala-Phe-Val-Gly-Tyr-Val-Leu-Pro and Glu-Lys-Ser-Tyr-Glu-Leu-Pro. The first peptide displayed the highest ACE inhibitory activity with an IC 50 of 5.22 lM. Lineweaver-Burk plots suggest that Val-Glu-Leu-Tyr-Pro acts as a non-competitive inhibitor against ACE. Furthermore, antihypertensive effects in spontaneously hypertensive rats (SHR) also revealed that oral administration of Val-Glu-Leu-Tyr-Pro can decrease systolic blood pressure significantly (p < 0.01). These results suggest that the Val-Glu-Leu-Tyr-Pro would be a beneficial ingredient for nutraceuticals and pharmaceuticals acting against hypertension and its related diseases.
Food Research International, 2010
The angiotensin I-converting enzyme (ACE) inhibitory activities of protein hydrolysates prepared from muscle of cuttlefish (Sepia officinalis) by treatment with various digestive proteases were investigated. The most active hydrolysate was obtained with the crude protease extract from the hepatopancreas of cuttlefish (64.47 ± 1.0% at 2 mg of dry weight/ml) with a degree of hydrolysis of 8%. By gel filtration on Sephadex G-25 and RP-HPLC on C18 column, three novel peptides with high ACE-inhibitory activity were purified and their molecular masses and amino acid sequences were determined. The three peptides Val-Tyr-Ala-Pro, Val-Ile-Ile-Phe and Met-Ala-Trp with IC 50 values of 6.1, 8.7 and 16.32 lM, respectively, were novel ACE-inhibitory peptides. Lineweaver-Burk plots suggest that the three purified peptides act as noncompetitive inhibitors against ACE. These results suggest that some peptides from cuttlefish could be a beneficial ingredient for nutraceuticals against hypertension.
Journal of Food Science, 2000
Angiotensin I-converting enzyme (ACE)-inhibitory peptides from the thermolysin digest of chicken muscle and the peptic digest of ovalbumin were isolated. However, some of them failed to show antihypertensive activity in spontaneously hypertensive rats (SHR). To clarify this discrepancy, ACE-inhibitory peptides from various sources were preincubated with ACE before measurement of ACE-inhibitory activity and classified into 3 groups: (1) inhibitor type, IC 50 values of peptides that are not affected after preincubation with ACE;( 2) substrate type, peptides that are hydrolyzed by ACE to give peptides with weaker activity; and (3) prodrug-type inhibitor, these peptides are converted to true inhibitors by ACE or gastrointestinal proteases. Peptides belonging to the 1st and the 3rd groups exert antihypertensive activities even after oral administration in SHR.
Food chemistry, 2015
An alkaline extracted brewers' spent grain protein-enriched isolate (BSG-PI) was hydrolysed using Alcalase, Corolase PP, Flavourzyme and Promod 144MG, yielding Alc hydrolysate (H), CorH, FlavH and ProH, respectively. The degree of hydrolysis (DH) of the protein hydrolysates varied from 4.45% for ProH to 16.4% for CorH. The in vitro ACE inhibitory activity of the BSG-PI increased significantly following 15min incubations with Alcalase, Corolase PP and Flavourzyme. The 5kDa ultrafiltration permeates of FlavH and CorH resulted in lower ACE IC50 values than their respective hydrolysates. The bioactivity of the BSG-PI hydrolysates was retained after simulated gastrointestinal digestion (SGID) while SGID also resulted in the release of ACE inhibitory peptides from the BSG-PI and ProH. UPLC-MS/MS analysis resulted in the identification of 34 peptides. Of 12 synthesised peptides, IVY and ILDL were the most potent, having ACE IC50 values at 80.4±11.9 and 96.4±8.36μM, respectively.