Angiotensin Converting Enzyme (ACE) Inhibitory Peptides: Production and Implementation of Functional Food (original) (raw)
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Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology
The existence of endogenous bioactive protein or peptide with angiotensin-converting enzyme (ACE) inhibitory activity in snakehead meat is promising to be investigated. The purposes of this research were to extract ACE inhibitory endogenous bioactive protein or peptide from snakehead meat and to fractionate the active compounds using ultrafiltration. The extraction in this research employs two kinds of solvents, e.i aquadest and 50% ethanol. Then, the extract is fractionated with the ultrafiltration using the 10,000; 5,000 and 3,000 MWCO membranes to separate the protein or peptide of with the sizes of >10 kDa, 5 – 10 kDa, 3 – 5 kDa and <3 kDa. The parameters being observed from the crude extracts and its fractions included the protein and peptide content, the ACE inhibitory activity (in vitro), and the protein and peptide profiles determined by using the SDS PAGE. The result of this research revealed that the snakehead meat contained ACE inhibitory endogenous bioactive prote...
Food Research, 2023
In the fish processing sector, fish have been processed in large quantities, are generated and discarded into the sea or dumped into the oceans. However, by employing effective strategies, this fishery waste can be utilized and converted into fish protein hydrolysate (FPH). FPH is a rich source of amino acids and peptides that have biological properties such as angiotensin-converting enzyme (ACE) inhibition, antimicrobial, antioxidant, and anticancer activity. The FPH has been used as a functional food perspective related to improving human health, primarily by maintaining blood pressure and normal heart function as measured by antihypertensive activity. FPH can be produced by various fish species, parts, and hydrolysis methods. Several studies have been published on the acceptability of FPH in obtaining bioactive properties from various fish, each using a different method to obtain bioactive properties. FPH is commonly produced by fish species such as Atlantic Cod, Lizard Fish, Atlantic Chub Mackerel, Atlantic Horse Mackerel, and Kawakawa (Mackerel Tuna). Furthermore, we summarized the various methodologies used by various researchers based on raw material data collection, method of production, ACE-inhibitory assay, ACE-inhibitory activity, degree of hydrolysis, molecular weight, purification method, and ACE-I peptide structure in this review.
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.
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. #
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!
Bioresource Technology, 2005
The angiotensin I converting enzyme (ACE) inhibitory activity of fermented blue mussel sauce (FBMS) was investigated. Blue mussels were fermented with 25% NaCl (w/w) at 20°C for 6 months and the resultant mixture was passed through a 40-mesh sieve, desalted using an electrodialyzer and then lyophilized. The IC 50 value of FBMS for ACE activity was 1.01 mg/ml. An ACE inhibitory peptide was purified from FBMS using Sephadex G-75 gel chromatography, SP-Sephadex C-25 ion exchange chromatography and reversed-phase high-performance liquid chromatography on a C 18 column. The IC 50 value of purified ACE inhibitory peptide was 19.34 lg/ml, and 10 amino acid residues of the N-terminal sequence was EVMAGNLYPG. The purified peptide was evaluated for antihypertensive effect in spontaneously hypertensive rats (SHR) following oral administration. Blood pressure significantly decreased after peptide ingestion. This result suggested that FBMS may have beneficial effects on hypertension.
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 (...
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.
In this study, soft-shelled turtle (Pelodiscus sinensis) egg white (SSTEW) proteins were digested by thermolysin and the resulting small peptides were further fractionated by reverse phase chromatography. Peptides with angiotensin I-converting enzyme inhibitory (ACEI) activity from these fractions were screened. A lysozyme-derived peptide, IW-11, from the fraction with the most effective ACEI was identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and its purified form showed effective ACEI activity in vitro (IC 50 = 4.39 ± 0.31 μM). The Lineweaver-Burk plots indicated that the inhibition towards ACE caused by this peptide is a competitive inhibition. The molecular docking study further revealed that the ACEI activity of IW-11 is mainly attributed to the formation of hydrogen bonds between the N-terminal residue of IW-11 and the S1 pocket (Ala354 and Tyr523) and the S2′ region (His513 and His353) of ACE. Moreover, the digestion parameters were further optimized and the target peptide (82% purity) was readily obtained (15% yield) without any cumbersome purification procedure. Notably, lysozyme C is the most abundant protein in SSTEW, which implies that an efficient production of this ACEI peptide from SSTEW is promising.