Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Daşkaya-Dikmen, Ceren; Yücetepe, Aysun; Karbancıoğlu-Güler, Funda; Daşkaya, Hayrettin; Özçelik, Beraat

doi:10.3390/nu9040316

Cited by 237 publications

(169 citation statements)

References 122 publications

(277 reference statements)

Supporting

Mentioning

165

Contrasting

Unclassified

Order By: Relevance

“…In addition, microencapsulation of hydrolysates plus incorporation of masking agents are effective alternatives for attenuation of bitterness in hydrolysates. Daskaya-Dikmen et al (2017) claimed that encapsulation of peptides in hydrolysates is the most favorable technique in order to reduce bitterness. Favaro-Trindade et al (2010) reported that bitter taste decreased when casein hydrolysates were spray-dried and mixed with gelatin and soy protein isolate as carriers.…”

Section: Removing Bitternessmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

133

View full text Add to dashboard Cite

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.

show abstract

Section: Removing Bitternessmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

133

View full text Add to dashboard Cite

show abstract

“…As previously reported, ACE-inhibitory activity of peptides is affected by their amino acids content. Potent ACE-inhibitory peptides contain short amino acids sequence between 2-12 residues and crystallographic studies have shown that large peptides may not bind to the active sites of ACE (23 - 25). The type of amino acids could be more relevant than the length of the peptide sequence.…”

Section: Resultsmentioning

confidence: 99%

“…Majority of the previously reported ACE-inhibitory peptides derived from food sources contain pro and aromatic amino acids such as Tyr, Tryp or Phe at their C terminal (4, 16, 24, 28) and/or branched aliphatic amino acids such as Val, Leu, Ile at their N terminal (23). The positively charged amino acids arginine (R) and lysine (K) present at the C-terminal were also found to contribute to the ACE inhibitory potency of peptides (29).…”

Section: Resultsmentioning

confidence: 99%

Identification, structure-activity relationship andin silicomolecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish hydrolysates

Auwal

Abidin

Zarei

et al. 2018

Preprint

View full text Add to dashboard Cite

Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including ALGPQFY (794.44 Da), KVPPKA (638.88 Da), LAPPTM (628.85 Da), EVLIQ (600.77 Da) and EHPVL (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.31 mM, 1.44 mM and 1.68 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.

show abstract

“…A large number of literatures have reported that the chain length, amino acid composition, amino acid sequence and spatial structure have a great influence on the activity of ACE inhibitory peptide. Long peptides are difficult to bind to the active sites of ACE, so most of the high active ACE inhibitory peptides have a chain length of 2-12 amino acids, the lower the molecular weight (<3kDa), the higher the inhibitory activity [36,60,61]. However, in many cases, the influence of amino acid type and sequence on ACE inhibitory activity of peptide is much greater than that of peptide chain length.…”

Section: Antihypertensive Active Peptidementioning

confidence: 99%

Bioactive Peptides from Walnut Residue Protein

Guo

Chi

et al. 2020

Molecules

View full text Add to dashboard Cite

Walnut residue is a kind of high-quality plant protein resource. The bioactive peptide prepared from walnut residue has excellent health care functions such as antioxidation and antihypertensive activity, but at present, walnut residue is often regarded as waste or low value feed, fertilizer and other materials. The uneconomical use of walnut residue has hindered the development of the walnut industry to some extent. Effective utilization of walnut residue protein to develop bioactive peptides and other products is of great significance to realize the comprehensive utilization of walnut residue, improve the added value of by-products, and change the current low utilization rate of walnut residue. In this paper, the preparation, purification and structure identification of walnut protein bioactive peptides are reviewed, and different functional walnut active peptides (WBPs) are introduced. The potential effects of these bioactivities on human health and their different uses in food, medicine and other industries are discussed. The purpose is to provide reference information for the effective utilization of walnut residue resources and the development of walnut industry.

show abstract

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Cited by 237 publications

References 122 publications

Peptides: Production, bioactivity, functionality, and applications

Peptides: Production, bioactivity, functionality, and applications

Identification, structure-activity relationship andin silicomolecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish hydrolysates

Bioactive Peptides from Walnut Residue Protein

Contact Info

Product

Resources

About