Functional and potential therapeutic ACE-inhibitory peptides derived from bromelain hydrolysis of trevally proteins

Salampessy, Junus; Reddy, N. Venkata; Kailasapathy, Kasipathy; Phillips, Mike

doi:10.1016/j.jff.2015.02.037

Cited by 58 publications

(28 citation statements)

References 47 publications

(47 reference statements)

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“…On the other hand, the IC50 value of ACE inhibitory activity of TSMH in the current study was found to be 1.5 mg/mL which was 6 times lower than that for control. This IC50 level was comparable with the IC50 values reported for Goby fish protein hydrolysate [19], but lower than those for rice bran protein hydrolysate (5.2 mg/mL) and bromelain-hydrolyzed trevally protein (1.99 to 3.34 mg/mL) [20]. Sheep whey protein hydrolysate obtained after hydrolysis using partially purified protease from B. subtilis showed 57% ACE inhibitory activity at 50 mg/mL concentration [21].…”

Section: Ace-inhibitory Activity Of Tsmhsupporting

confidence: 77%

ACE-Inhibitory and Antioxidant Activities of Peptide Fragments Obtained from Tomato Processing By-Products Fermented Using Bacillus subtilis: Effect of Amino Acid Composition and Peptides Molecular Mass Distribution

Moayedi

Mora

Aristoy

et al. 2016

Appl Biochem Biotechnol

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The effects of amino acid composition and peptide molecular mass on ACE-inhibitory and antioxidant activities of protein fragments obtained from tomato waste fermented using Bacillus subtilis were evaluated. The addition of B. subtilis increased the relative amounts of aromatic and positively-charged amino acids which have been described to influence the biological activities of peptide fragments. IC values of hydrolysates for ACE-inhibitory and 2, 2'-diphenyl-1-picrylhydrazyl (DPPH) scavenging activities were found to be 1.5 and 8.2 mg/mL, respectively. Size-exclusion chromatography (SEC) pattern of the hydrolysate indicated the breakdown of parent proteins to smaller peptides with molecular weights mainly below 1400 Da. MALDI-TOF mass spectrometry analysis revealed that the highest ACE-inhibitory activity was due to peptides showing molecular mass range 500-800 Da, while the most active antioxidant peptides were found to be mainly at the two different peptide weight ranges 500-800 Da and 1200-1500 Da.

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Section: Ace-inhibitory Activity Of Tsmhsupporting

confidence: 77%

ACE-Inhibitory and Antioxidant Activities of Peptide Fragments Obtained from Tomato Processing By-Products Fermented Using Bacillus subtilis: Effect of Amino Acid Composition and Peptides Molecular Mass Distribution

Moayedi

Mora

Aristoy

et al. 2016

Appl Biochem Biotechnol

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“…There were nine peptides (GHIITVAR, IGGIGTVPVGR, FMPGVPGPIQR, PNYHPSPR, HIITLGR, LAGNPAGR, MPGVPGPIQR, AGALGDSVTVTR, INTLSGR) containing Arg in this study (Table 3). Arg is a basic aliphatic amino acid and also a positively charged amino acid, which was most frequently observed at the C-terminal of the ACE inhibitory peptides according to a lot of studies, such as YR and IR from the hydrolysates of marine sponge [36], APER from trevally hydrolysate [37]. It was noteworthy that the peptide GHIITVAR exhibiting the lowest IC 50 value of 3.60 ± 0.10 µM among the 11 peptides.…”

Section: Characterization Of Ace Inhibitory Peptide By Nano Uhplc-esimentioning

confidence: 98%

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

Wang

Lü

Sun

et al. 2020

IJMS

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The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.

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“…Although crude proteases extracts (e.g., from fish) have been successfully used as catalysts in enzymatic hydrolysis Lassoued et al, 2015b), commercially purified enzymes are preferably employed since they allow a better control over the hydrolysis process (e.g., shorter reaction time for a desired DH, more consistent peptides size and composition) (Samaranayaka and Li-Chan, 2011). Consequently, industrial proteases derived from different sources such as microorganisms (e.g., Alcalase, Neutrase, Protease P "Amano" 6, Flavourzyme, Protamex) (Halldorsdottir et al, 2013;Venuste et al, 2013), animals (e.g., PTN, pepsin, trypsin, a-chymotrypsin, pancreatin) (Wu et al, 2015a, b;Garc ıa-Moreno et al, 2017) and plants (e.g., papain, bromelain) (Salampessy et al, 2015;Elavarasan et al, 2016) have been widely employed for the production of protein hydrolysates exhibiting bioactive and/or functional properties. These marketable proteases may mainly contain endopeptidases (e.g., trypsin, subtilisin, papain), or a combination of endopeptidases and exopeptidases (e.g., carboxypeptidases, aminopeptidases).…”

Section: Enzymatic Protein Hydrolysismentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

138

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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Functional and potential therapeutic ACE-inhibitory peptides derived from bromelain hydrolysis of trevally proteins

Cited by 58 publications

References 47 publications

ACE-Inhibitory and Antioxidant Activities of Peptide Fragments Obtained from Tomato Processing By-Products Fermented Using Bacillus subtilis: Effect of Amino Acid Composition and Peptides Molecular Mass Distribution

ACE-Inhibitory and Antioxidant Activities of Peptide Fragments Obtained from Tomato Processing By-Products Fermented Using Bacillus subtilis: Effect of Amino Acid Composition and Peptides Molecular Mass Distribution

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

Peptides: Production, bioactivity, functionality, and applications

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