ACE Inhibitory Peptides Derived from Enzymatic Hydrolysates of Animal Muscle Protein: A Review (original) (raw)
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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. #
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.
Insects as source of angiotensin converting enzyme inhibitory peptides
Journal of Insects as Food and Feed, 2017
Hypertension is well known as one of the major risk for cardiovascular diseases which annually affect millions of people. The angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation process. Indeed, hypertension treatment by synthetic ACE inhibitors (e.g. captopril, lisinopril and ramipril) is effective; however, their use can cause serious side effects, such as hypotension, cough, reduced renal function and angioedema. Thus, research was focused on natural ACE inhibitory peptides sources such as foodstuffs and also, more recently, edible insects. In the last decades, ACE inhibitory activity has been detected in protein hydrolysates from insect species belonging to the orders of Coleoptera, Diptera, Hymenoptera, Lepidoptera and also Orthoptera. Further investigations led to identify specific ACE inhibitory peptides from the silkworm Bombyx mori (Lepidoptera: Bombycidae), the yellow mealworm Tenebrio molitor (Coleoptera: Tenebrionidae), the cotton leafworm S...
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.
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.
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 (...
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.
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.
International Journal of Peptide Research and Therapeutics, 2020
Hypertension is declared as the major risk factor of cardiovascular diseases and stroke, and the leading cause of premature deaths. ACE is a zinc dependent dipeptidyl peptidase and plays key role in controlling blood pressure via renin angiotensin system (RAS), and hence serves as the promising target for antihypertension drugs. Many food derived antihypertensive peptides have been identified recently. However, their ACE inhibitory activity, interactions and stability are not fully evaluated. Our work focused on combination of modern bioinformatics techniques for efficient evaluation of potent ACE inhibitory food peptides and understanding of interactions between ACE and inhibitory peptides. We reported novel antihypertensive peptide IQDVPS, LQPGS, VIP from date, salmon and soybean proteins respectively. Food proteins were digested in-silico to release peptides. Molecular docking studies revealed high binding affinities and interactions with ACE active site. MD simulations and Alanine Scanning were carried out to study the stability of these ACE-peptide complexes in cell like environment. The results showed that the suggested peptides competitively inhibit ACE by tightly binding to its active site, meanwhile maintaining the structural stability of the complex. ACE-LQPGS (Salmon) was found to have best binding with least structural fluctuations.