The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme

Tsai, Jung‐Hui; Lin, T.C.; Chen, J.L.; Pan, Bonnie Sun

doi:10.1016/j.procbio.2006.05.023

Cited by 111 publications

(66 citation statements)

References 19 publications

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“…All inhibitors cause the substrate to react at a lower rate than without the inhibitor (Lee et al, 2010). Although most reported peptide inhibitors of ACE acted as competitive inhibitors, a few have exhibited noncompetitivetype ACE inhibition (Tsai et al, 2006). The purified peptide in this study also exhibited an inhibition pattern of being able to bind to the active site.…”

Section: Ace Inhibitory Activity Of Hydrolysatesmentioning

confidence: 73%

“…Moreover, the ACE inhibitory peptide from oyster was also found to be competitive (Je et al, 2005 a) along with other types such as rotifer (Lee et al, 2009). Captopril has been reported to show competitive inhibition with the substrate for binding to active ACE site (Tsai et al, 2006). These competitive inhibitors are able to enter the ACE protein molecule, interact with the active sites and prevent substrate binding (Jiang et al, 2010).…”

Section: Ace Inhibition Pattern Of Purified Peptidesmentioning

confidence: 99%

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The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

Kim¹,

Byun

2012

Fisheries and aquatic sciences

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The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The IC 50 value of purified ACE inhibitory peptide was 63.9 μM. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-SerPro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

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Section: Ace Inhibitory Activity Of Hydrolysatesmentioning

confidence: 73%

Section: Ace Inhibition Pattern Of Purified Peptidesmentioning

confidence: 99%

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

Kim¹,

Byun

2012

Fisheries and aquatic sciences

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“…In connection with this, Wu et al (2002) have reported that the spectrophotometric assay described by Cushman and Cheung (1971), widely used for testing ACE inhibition of gelatin hydrolysates, tends to overestimate the amount of HA produced during ACE-catalyzed reactions. Having this in mind, IC 50 values of the most potent inhibitor (peptide I), were between 26-and 1.5-fold higher than those reported for ACE inhibitory peptides derived from different food proteins, tested in similar conditions (Centeno et al, 2006;He, Chen, Sun, Zhang & Zhou, 2006;Tsai, Lin, Chen, & Pan, 2006;Tauzin, Miclo, & Gaillard, 2002). Therefore, peptide I could be considered as a moderate ACE inhibitory peptide.…”

Section: Ace Inhibitory Activity Of Synthetically Derived Peptidesmentioning

confidence: 79%

Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate

et al. 2011

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** This centre has implemented and maintains a Quality Management System which fulfils the requirements of the ISO standard 9001:2000 AbstractSquid gelatin obtained from inner and outer tunics was hydrolyzed with Alcalase to isolate antioxidant peptide sequences. The ACE-inhibitory activity of the isolated peptides was also evaluated. After fractionation by ultrafiltration and size-exclusion chromatography into four fractions, the antioxidant activity of the peptide fractions was determined by radical scavenging ability and ferric reducing power. Fraction FIII showed the highest antioxidant activity, although slight differences could be expected in the antioxidant activity of the different fractions based on the amino acid composition.FIII was subjected to liquid chromatography and tandem mass spectrometry (LC-MS/MS) and two major compounds were identified: the compound with m/z 952.42, which could be mostly comprised by the carbohydrate fucose, and the peptide with m/z 1410.63. Three possible sequences were proposed for this peptide, and the contribution of Leu or Hyp residues to the antioxidant and ACE-inhibitory activities of the resulting sequence was evaluated. The presence of Leu residues in the peptide sequence in *Manuscript Click here to view linked References 2 replacement of Hyp seems to play an important role in the antioxidant and ACEinhibitory activity.

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“…The low peptide content was related to the type of enzyme used and the specific action of that enzyme in the separation of peptide bonds in the sample. [24] reported that the peptide content was influenced by the specific action of the enzyme used in the separation of peptide bond. The highest peptides content was recorded by EBN hydrolyzed by pancreatin enzyme at 1.0 hour of hydrolysis time with 109.5 mg/g and the lowest was recorded by EBN hydrolyzed by alcalase at 0.5 hour of hydrolysis time with 81.2mg/g.…”

Section: Peptide Contentmentioning

confidence: 99%

Effect of enzymatic hydrolysis of pancreatin and alcalase enzyme on some properties of edible bird’s nest hydrolysate

Khushairay¹,

Ayub²,

Babji³

2014

AIP Conference Proceedings

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Abstract. Edible bird nest (EBN) is a dried glutinous secretion from the salivary glands of several different swiftlet species. It is widely consumed as a health food due to its high beneficial effects to human health and has been considered to be one of the most precious food items by the Chinese for thousands of years. The aim of this study was to evaluate the effect of enzymatic hydrolysis on protein solubility (μg/g), the degree of hydrolysis (DH%), and peptide content (μg/g) of edible bird's nest hydrolysate. Initial protein solubility of boiled EBN was 25.5mg/g EBN. Treating the solubilized EBN with pancreatin 4NF for 1.0 -1.5hours increased EBN protein solubility to 163.9mg/g and produced hydrolysate with DH% of 86.5% and 109.5mg/g peptide. EBN hydrolyzed with alcalase for 1.5 hours produced hydrolysate with protein solubility of 86.7mg/g, 82.7 DH% and had 104.1mg/g peptide content.

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The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme

Cited by 111 publications

References 19 publications

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate

Effect of enzymatic hydrolysis of pancreatin and alcalase enzyme on some properties of edible bird’s nest hydrolysate

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