Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast

Sangsawad, Papungkorn; Roytrakul, Sittiruk; Yongsawatdigul, Jirawat

doi:10.1016/j.jff.2016.12.005

Cited by 74 publications

(49 citation statements)

References 29 publications

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“…Bioactive peptides have been also isolated from meat using bacterial, animal and plant proteases [1,10]. However, there is a considerable lack of information regarding the peptides released after in vitro digestion of cooked meat since only a few studies have been designed to fill this gap [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion

Martini

Conte

Tagliazucchi

2019

Journal of Proteomics

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This study was designed to investigate the potential contribution of bioactive peptides to the biological activities related to the consumption of pork, beef, chicken and turkey meat following in vitro gastro-intestinal digestion. After extraction of the peptidic fractions from digested samples, the bioactivities were evaluated by in vitro antioxidant activity as well as angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) inhibition assays. Pork and turkey meat appeared to be the best sources of antioxidant peptides. Pork was found to be the best source of DPP-IV-inhibitory peptides whereas chicken meat supplied peptides with the highest ACEinhibitory activity. The comprehensive analysis of the peptidomic profile of digested samples was performed by nano-LC-ESI-QTOF MS/MS analysis. A total of 217, 214, 257 and 248 peptides were identified in digested pork, beef, chicken and turkey meat, respectively. Chicken and turkey meat showed the highest similarity in peptide sequences with 202 common peptides. Sixty-two peptides matched with sequences with previously demonstrated biological activity. In particular, 35 peptides showed ACE-inhibitory activity and 23 DPP-IV inhibitory activity. Twenty-two bioactive peptides were commonly released from the different types of meat. The relative amount of identified bioactive peptides were positively correlated to the biological activities of the different digested meats.

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Section: Introductionmentioning

confidence: 99%

Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion

Martini

Conte

Tagliazucchi

2019

Journal of Proteomics

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“…Iroyukifujita et al (2000) checked the IC 50 value of chicken muscle hydrolysate under the thermolysin digestion, where seven ACE-inhibitory peptides with the sequence of LKA, LKP, LAP, IKW, FQKPKR, FKGRYYP and IVGRPRHQG were isolated along with the IC 50 values ranging from 0.21 to 14 lM. Under the GI digestion in vitro, KPLLCS, ELFTT and KPLL were isolated in the breast of Korat chicken with IC 50 values of 0.37, 6.35 and 11.98 lM, respectively (Sangsawad et al, 2017). Although KPLLCS was investigated to be the most effective ACE inhibitor, the degradation was inevitable in the Caco-2 cell monolayer.…”

Section: Anti-hypertensive Peptidesmentioning

confidence: 99%

Meat protein based bioactive peptides and their potential functional activity: a review

Xing

Cao

et al. 2019

Int J of Food Sci Tech

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Summary Bioactive peptides are the general name for the short amino acid sequences, which could be generated from the hydrolysis of parent proteins including beef, pork, mutton, chicken, duck and various species of marine organisms. Drying, curing, ripening and fermentation are particular procedures for meat flavour and also important for the releasing of bioactive peptides from parent proteins. Once being released, the peptides would play bioactive roles beyond their nutritional values. The physiological activities of meat‐derived peptides have been demonstrated to have antioxidative, antihypertensive, antimicrobial, opioid, antithrombotic and other bioactive effects. The regulation on immunological, gastrointestinal and neurological responses of those bioactive peptides supplies a vital base for the prevention of hypertension, obesity, diabetes and other metabolic disorders. In this review, we summarised the current studies on meat derived bioactive peptides along with their physiological functions to supply the overall understanding of the health benefit of bioactive peptides.

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“…The ACE inhibitory peptides were purified according to the method described by Sangsawad et al [12], with slight modifications. The fraction showing the highest ACE inhibitory activity was redissolved in distilled water at a concentration of 30 mg/mL and subjected to further purification using the Sephadex G-15 column (1 × 50 cm), which was eluted using distilled water at a flow rate of 1 mL/min.…”

Section: Gel Filtration Chromatographymentioning

confidence: 99%

Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (<i>Corylus heterophylla</i> Fisch) Protein

Yu¹,

Liu²,

You³

2019

FNS

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Although a number of bioactive peptides are capable of angiotensin I-converting enzyme (ACE) inhibitory effects, little is known regarding the mechanism of hazelnut peptides using molecular simulation. In the present study, gel filtration chromatography, reverse phase-high performance liquid chromatography, and liquid chromatography-electrospray ionization-tandem mass (LC-ESI-MS/MS) were employed for purifying and identifying the ACE inhibitory peptides from hazelnut. To understand the mode of action of these peptides, the interaction between the inhibitory peptides and ACE was investigated. The results identified novel ACE inhibitory peptides Asp-Asp-Glu-Leu-Arg-Gln-Ala (DDELRQA), Asp-Asp-Glu-Leu-Arg-Ala-Ala (DDELRAA), and Asp-Gly-Glu-Leu-Arg-Glu (DGELRE). The binding free energies of DDELRQA, DDELRAA, and DGELRE for ACE were −10.2, −9.0, and −8.8 kcal/mol, respectively. This study proves the high stability of ACE inhibitory peptides derived from hazelnut against different temperature and pH of processing.

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Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast

Cited by 74 publications

References 29 publications

Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion

Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion

Meat protein based bioactive peptides and their potential functional activity: a review

Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (<i>Corylus heterophylla</i> Fisch) Protein

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Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast

Cited by 74 publications

References 29 publications

Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion

Comparative peptidomic profile and bioactivities of cooked beef, pork, chicken and turkey meat after in vitro gastro-intestinal digestion

Meat protein based bioactive peptides and their potential functional activity: a review

Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (&lt;i&gt;Corylus heterophylla&lt;/i&gt; Fisch) Protein

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Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (<i>Corylus heterophylla</i> Fisch) Protein