Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales

Fahmi, Abdelgawad A.; Morimura, Shigeru; Guo, Huiqing; Shigematsu, Toru; Kida, Kenji; Uemura, Yohnosuke

doi:10.1016/s0032-9592(03)00223-1

Cited by 172 publications

(99 citation statements)

References 18 publications

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“…Inhibition potencies of alcalase digest of skin (IC 50 0870 μg/ml) and bone (IC 50 0710 μg/ml) gelatin before fractionation were significantly higher than untreated skin (IC 50 01680 μg/ml) and bone (IC 50 01550 μg/ml) gelatin (Table 1). The ACE inhibition activity of skin and bone gelatin hydrolysates in the present study were almost similar with that of alaska pollack skin (IC 50 0629 μg/ml) , skate skin (IC 50 0680 μg/ml) (Lee et al 2011), sardinella byproduct (IC 50 0810 μg/ml) (Bougatef et al 2008) and sea bream scales (IC 50 0570 μg/ml) (Fahmi et al 2004) protein hydrolysates. Results of this study indicated that by increasing the MWCO size, ACE inhibition activity of fractions were increased.…”

Section: Degree Of Hydrolysis (%)supporting

confidence: 78%

“…Several natural ACE inhibitory peptides have been isolated from collagen and gelatin enzymatic hydrolysate of various food protein sources such as porcine skin collagen (Ichimura et al 2009), bovine skin gelatin , fish skins Nagai et al 2006;Park et al 2009), fish cartilage (Nagai et al 2006), scales (Fahmi et al 2004), squid (Alemán et al 2011) and sea cucumbers protein hydrolysates (Zhao et al 2007) as an alternative approach to the synthetic ACE inhibitory drugs.…”

Section: Introductionmentioning

confidence: 99%

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ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

et al. 2012

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Skin and bone gelatins of pangasius catfish (Pangasius sutchi) were hydrolyzed with alcalase to isolate Angiotensin Converting Enzyme (ACE) inhibitory peptides. Samples with the highest degree of hydrolysis (DH) were separated into different fractions with molecular weight cutoff (MWCO) sizes of 10, 3 and 1 kDa, respectively and assayed for ACE inhibitory activity. Skin and bone gelatins had highest DH of 64.87 and 68.48 % after 2 and 1 h incubation, respectively. Results from this study indicated that by decreasing the molecular weight of fractions, ACE inhibitory activity was increased. Therefore, F 3 permeates (MWCO< 1 kDa) of skin (IC 50 03.2 μg/ml) and bone (IC 50 01.3 μg/ml) gelatins possessed higher ACE inhibitory activity compared to their untreated gelatins and corresponding hydrolyzed fractions. In this study, the major amino acids were Glycine followed by Proline with an increased amount of hydrophobic amino acid content in F 3 permeates of skin (4.01 %) and bone (5.79 %) gelatin. Digestion stability against gastrointestinal proteases did not show any remarkable change on ACE inhibition potency of these permeates. It was concluded that alcalase hydrolysis of P. sutchi by-products could be utilized as a part of functional food or ingredients of a formulated drug in order to control high blood pressure.

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Section: Degree Of Hydrolysis (%)supporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

et al. 2012

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“…The antihypertensive effects of collagen hydrolysates prepared from various sources and the isolation of several ACE inhibitory peptides from those hydrolysates have been reported in previous works (Byun Fahmi et al, 2004;Zhao et al, 2007;Saiga et al, 2008;Ichimura, Yamanaka, Otsuka, Yamashita & Maruyama, 2009). However, the use of different methods and their associated modifications to test ACE inhibitory capacity makes difficult the direct comparison of IC 50 values from different studies when some reports do not detail the number of enzyme units used in the inhibition analysis or do not include an IC 50 value for an ACE inhibitory standard such as Captopril® (Murray, Walsh & FitzGerald, 2004).…”

Section: Ace Inhibitory Activity Of Synthetically Derived Peptidesmentioning

confidence: 60%

“…However, to the best of our knowledge, ACE-inhibitory capacity has not been described in squid skin gelatin hydrolysates, although this activity has been reported in collagen and gelatin hydrolysates from other marine species (Kim, Byun, Park & Shahidi, 2001;Fahmi, Morimura, Guo, Shigematsu, Kida & Uemura, 2004;Kim & Mendis, 2006;Zhao, Li, Liu, Dong, Zhao & Zen, 2007).…”

Section: Introductionmentioning

confidence: 91%

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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“…Those values measured by the conventional method with HHL are also given in Table 1 for the purpose of a comparison. [10][11][12][13][14][15][16][17][18] The published data were over a wide range because the IC50 values were influenced by various factors, including the method conditions, the source of the enzyme, the calculation method, and the relationship between the inhibitor and the enzyme source. 1,11 Thus, it was difficult to compare the data directly, but the IC50 values recognized in this study did not differ vastly from the published data.…”

Section: Resultsmentioning

confidence: 99%

Assay of Angiotensin I-converting Enzyme-inhibiting Activity Based on the Detection of 3-Hydroxybutyrate with Water-soluble Tetrazolium Salt

et al. 2008

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A newly synthesized substrate, 3-hydroxybutyrylglycyl-glycyl-glycine (3HB-GGG), was applied to the assay of ACEinhibiting activity to overcome the smaller selectivity and sensitivity of the conventional method. In this study, an ACEinhibiting assay was improved by the use of a water-soluble tetrazolium salt, 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt (WST-1), for the detection of 3-hydroxybutyrate, derived from 3HB-GGG. The optimized conditions were as follows: 0.333 mM NAD + , 0.333 mM WST-1, 0.1 mM EDTA, 0.633 U ml -1 diaphorase, and 0.700 U ml -1 3-hydroxybutyrate dehydrogenase. The developed assay was efficiently applicable to evaluate the ACEinhibiting activity of practical ACE inhibitors.

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Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales

Cited by 172 publications

References 18 publications

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

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

Assay of Angiotensin I-converting Enzyme-inhibiting Activity Based on the Detection of 3-Hydroxybutyrate with Water-soluble Tetrazolium Salt

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