Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC–ESI-TOF MS/MS

Ghassem, Masomeh; Arihara, Keizo; Babji, Abdul Salam; Said, Mamot; Ibrahim, Saadiah

doi:10.1016/j.foodchem.2011.06.051

Cited by 93 publications

(56 citation statements)

References 28 publications

(37 reference statements)

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“…Table 2 shows a lower content of positively charged amino acids (Arg, Lys, His) in F 3 fractions of P. sutchi skin and bone gelatins in comparison to their untreated gelatins and hydrolysates. These results were in agreement with those reported by Wu et al 2008 andGhassem et al 2011b. Therefore, the high ACE inhibitory potency of F 3 fractions of skin (IC 50 03.2 μg/ml) and bone (IC 50 01.3 μg/ml) gelatins could be due to the high content of hydrophobic amino acid residues in their peptidic fragments.…”

Section: Degree Of Hydrolysis (%)supporting

confidence: 92%

“…Alcalase manifested extensive proteolytic activity during the hydrolysis of skin gelatin from Alaska pollack, squid Todarodes pacificus and giant squid, producing hydrolysates with low average molecular weight which exhibited high ACE inhibitory capacity (Giménez et al 2009;Nam et al 2008). Several reports have indicated that ultrafiltrated hydrolysates composed of short-chain peptides with very low molecular weights contained remarkably high in vitro ACE inhibitory activity (Ghassem et al 2011b;Li and Aluko 2010;Pan et al 2012;Segura-Campos et al 2011), which coincided well with the current report. Similar findings were also observed for enzymatic digests of whey proteins where ultrafiltrated peptide fractions with molecular weight less than 3 kDa (Mullally et al 1997) and 1 kDa (Fujita et al 2000) possessed higher ACE inhibitory activity than their hydrolysates.…”

Section: Degree Of Hydrolysis (%)supporting

confidence: 91%

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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: 92%

Section: Degree Of Hydrolysis (%)supporting

confidence: 91%

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

et al. 2012

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“…Several researchers have identified the bioactive peptides from various protein hydrolysates using LC-MS/MS (Ghassem, Arihara, Babji, Said, & Ibrahim, 2011;Intarasirisawat, Benjakul, Wu, & Visessanguan, 2013;Théolier, Hammami, Labelle, Fliss, & Jean, 2013). The molecular weights of peptides from date seed protein hydrolysates dissolved in 0.1% TFA and 50 mM ammonium acetate in 2% CHCl3/methanol solvent system are presented in Table 3.…”

Section: Identification Of Peptides and Their Molecular Weightsmentioning

confidence: 99%

“…Li, Zhou, Huang, Sun, and Zeng (2012) reported that 20% of the world's adult population is affected by hypertension and related diseases such as stroke, coronary heart disease (CHD), kidney dysfunction, and myocardial infarction. Hypertension is regulated by the catalytic activity of a zinc protease, called angiotensin I converting enzyme (ACE) (Ghassem et al, 2011). ACE catalyzes the conversion of inactive angiotensin-I into a potent vasoconstrictor angiotensin-II and inactivates the vasodilator peptide bradykinin (Goodfriend, Elliott, &Catt, 1996 andKon, Fogo, Ichikawa, Hellings, &Bills, 1993).…”

Section: Hydroxyl Radical Scavengingmentioning

confidence: 99%

Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using Alcalase, Flavourzyme and Thermolysin

Ambigaipalan

Al‐Khalifa

Shahidi

2015

Journal of Functional Foods

165

160

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A B S T R A C TDate seed flour was used to produce protein hydrolysates using Alcalase (AL), Flavourzyme (FL) and Thermolysin (TH). Enzymes were used individually or in combination at a constant pH and temperature. The degree of hydrolysis ranged between 11 and 14%. The molecular weights of peptides determined, using a quadrupole orthogonal time-of-flight hybrid tandem mass spectrometer, ranged from 2062.9 ± 0.0 to 116,803.8 ± 0.4 Da. AL hydrolysate showed the lowest reducing power and ABTS radical scavenging activity, but a higher ACE inhibition and hydroxyl radical scavenging. Among all treatments, hydrolysates prepared using a combination of AL and FL exhibited the highest reducing power and metal chelation and high scavenging for ABTS, DPPH, hydroxyl radicals as well as ACE inhibitory activity. Combinations of AL and TH exhibited the highest ACE inhibitory activity with an IC50 value of 0.53 mg/mL. These results indicate that date seed protein hydrolysate could be used as a potential health promoting ingredient with antioxidant and ACE inhibitory activities.

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“…Purification was achieved by reverse phase high-performance liquid chromatography (RP-HPLC), and the peaks of the peptide absorbance were collected manually (Ghassem et al 2011). The RP-HPLC conditions were a 5-μm particle size Waters Spherisorb ® C 18 column, bonded silica 300°A pores, size 4.6 × 250 mm; a Water™ 717 plus autosampler, Water™ 600 controller, Water™ 600 pump, Water™ 996 Photodiode Array Detector (USA) using a Software Millenium version 2.1, a mobile phase of 50 % water (0.1 %, v/v, TFA) and 50 % MeOH running an isocratic gradient over a 1-h period at ambient temperature at a flow rate of 1.0 mL/min.…”

Section: Purification Methods By Rp-hplc and Identification By Tof Masmentioning

confidence: 99%

Novel antimicrobial peptide specifically active against Porphyromonas gingivalis

et al. 2015

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Porphyromonas gingivalis, the major etiologic agent of chronic periodontitis, produces a broad spectrum of virulence factors, including outer membrane vesicles, lipopolysaccharides, hemolysins and proteinases. Antimicrobial peptides (AMPs) including bacteriocins have been found to inhibit the growth of P. gingivalis; however, these peptides are relatively large molecules. Hence, it is difficult to synthesize them by a scale-up production. Therefore, this study aimed to synthesize a shorter AMP that was still active against P. gingivalis. A peptide that contained three cationic amino acids (Arg, His and Lys), two anionic amino acids (Glu and Asp), hydrophobic amino acids residues (Leu, Ile, Val, Ala and Pro) and hydrophilic residues (Ser and Gly) was obtained and named Pep-7. Its bioactivity and stability were tested after various treatments. The mechanism of action of Pep-7 and its toxicity to human red blood cells were investigated. The Pep-7 inhibited two pathogenic P. gingivalis ATCC 33277 and P. gingivalis ATCC 53978 (wp50) strains at a minimum bactericidal concentration (MBC) of 1.7 µM, but was ineffective against other oral microorganisms (P. intermedia, Tannerella forsythensis, Streptococcus salivarius and Streptococcus sanguinis). From transmission electron microscopy studies, Pep-7 caused pore formation at the poles of the cytoplasmic membranes of P. gingivalis. A concentration of Pep-7 at four times that of its MBC induced some hemolysis but only at 0.3%. The Pep-7 was heat stable under pressure (autoclave at 110 and 121 °C) and possessed activity over a pH range of 6.8-8.5. It was not toxic to periodontal cells over a range of 70.8-4.4 μM and did not induce toxic pro-inflammatory cytokines. The Pep-7 showed selective activity against Porphyromonas sp. by altering the permeability barriers of P. gingivalis. The Pep-7 was not mutagenic in vitro. This work highlighted the potential for the use of this synthetic Pep-7 against P. gingivalis.

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Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC–ESI-TOF MS/MS

Cited by 93 publications

References 28 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

Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using Alcalase, Flavourzyme and Thermolysin

Novel antimicrobial peptide specifically active against Porphyromonas gingivalis

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