Characterization and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from tilapia using Virgibacillus halodenitrificans SK1-3-7 proteinases

Tidarat, Toopcham; Roytrakul, Sittiruk; Yongsawatdigul, Jirawat

doi:10.1016/j.jff.2015.01.050

Cited by 56 publications

(41 citation statements)

References 43 publications

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“…Angiotensin‐converting enzyme inhibitory activity was measured using a spectrophotometric method with minor modifications as follows . The reaction mixture contained 50 μL 20 mmol L −1 HHL as a substrate, 50 μL of ACE powder (0.02 unit) in 150 mmol L −1 sodium borate buffer (pH 8.3), and 50 μL of sample solution.…”

Section: Methodssupporting

confidence: 88%

“…). Studies regarding structure–activity correlations among ACE inhibitory peptides revealed that hydrophobicamino acid, especially aromatic amino acids at the C‐terminus and branched chain amino acids at the N‐terminus, play a key role ininhibiting ACE activity . The peptides of P4‐3 identified here share some representative structural characteristics.…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, there are many studies devoted to simulating and building animal models similar to the human body, which have crucial research value and clinical significance . Angiotensin‐converting enzyme inhibitory peptides have been isolated successfully from various food proteins, such as those of olive flounder ( Paralichthys olivaceus ), tilapia, whey, and coconut, through fermentation and enzymatic hydrolysis. Some research not only obtained and identified ACE inhibitory peptides, but also fractionated tryptic casein hydrolysate using an ultra‐filtration membrane (3 kDa).…”

Section: Introductionmentioning

confidence: 99%

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Preparation and antagonistic effect of ACE inhibitory peptide from cashew

2019

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BACKGROUND Angiotensin‐converting enzyme (ACE) inhibitory peptides were found to alleviate acute hepatitis significantly. In this study, we purified and identified ACE inhibitory peptide from cashew to evaluate its protective role on alcohol‐induced acute hepatitis in mice. RESULTS The ACE inhibitory peptides were purified by using consecutive chromatographic techniques. One of these peptides (FETISFK) exhibited the highest ACE inhibition rate (91.04 ± 0.31%). In vivo, the results showed that ACE inhibitory peptide decreased levels of alanine aminotransferase (ALT) and aspartate aminotransferase (AST) caused by alcohol exposure. Moreover, it could increase the activities of superoxide dismutase (SOD) and glutathione (GSH), and decrease the level of malondialdehyde (MDA). It was also found to down‐regulate markedly the expression of interleukin‐6 (IL‐6) and tumor necrosis factor‐α (TNF‐α). It could also decrease the expression of ACE, angiotensin II (AngII) and angiotensin II type 1 receptor (AT1R). CONCLUSION These findings support the view that the ACE inhibitory peptide alleviated acute hepatitis by down‐regulating the ACE–AngII–AT1R axis, broadening the research approach to prevent acute hepatitis, and providing experimental data for the development and utilization of cashews. © 2019 Society of Chemical Industry

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Section: Methodssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Preparation and antagonistic effect of ACE inhibitory peptide from cashew

2019

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“…Hypertension is a major chronic disease affecting 30% of the adult population in the world [1]. Although there are many causes of hypertension, it is well recog-nized that angiotensin I-converting enzyme (ACE) plays an important role in the fluid and salt balance in mammals, as well as the rennin-angiotensin and the kallikrein-kinin systems for the regulation of blood pressure [2] [3].…”

Section: Introductionmentioning

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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“…Capriotti et al (2015) used the sequences of peptides identified by MS in fish protein hydrolysates to make queries in CAMP (http://www.bicnirrh.res.in/ antimicrobial) and BIOPEP databases. Toopcham et al (2015) used the peptides identified in tilapia protein hydrolysates as BIOPEP queries. To the Czech J.…”

mentioning

confidence: 99%

Carp proteins as a source of bioactive peptides - an in silico approach

Darewicz¹,

Borawska²,

Pliszka³

2016

Czech J. Food Sci.

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Darewicz M., Borawska J., Pliszka M. (2016): Carp proteins as a source of bioactive peptides -an in silico approach. Czech J. Food Sci., 34: 111-117.in silico prediction methods and tools were used to determine whether bioactive peptides are hidden in the amino acid sequences of carp (Cyprinus carpio) proteins and whether they can be released after gastric, duodenal, and gastroduodenal in silico digestion. Fragments with 15 types of biological activity in intact proteins and, after gastrointestinal digestion, with 11 types of activity were identified. Angiotensin I-converting enzyme inhibitory (ACEi) and antioxidant peptides were the most predominant fragments of proteins in the group of intact proteins and in silico digests. After in silico digestion the highest number of sequences with ACEi activity (108) and antioxidant activity (13) was released after gastro-duodenal digestion of the myosin heavy chain.

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Characterization and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from tilapia using Virgibacillus halodenitrificans SK1-3-7 proteinases

Cited by 56 publications

References 43 publications

Preparation and antagonistic effect of ACE inhibitory peptide from cashew

Preparation and antagonistic effect of ACE inhibitory peptide from cashew

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

Carp proteins as a source of bioactive peptides - an in silico approach

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Characterization and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from tilapia using Virgibacillus halodenitrificans SK1-3-7 proteinases

Cited by 56 publications

References 43 publications

Preparation and antagonistic effect of ACE inhibitory peptide from cashew

Preparation and antagonistic effect of ACE inhibitory peptide from cashew

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

Carp proteins as a source of bioactive peptides - an in silico approach

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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