Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
5.8
5.2
Journals
Foods
Special Issues
Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides
share announcement

Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Engineering and Technology".

Deadline for manuscript submissions: closed (10 August 2022) | Viewed by 15217

Special Issue Editors

Prof. Dr. Dong-Woo Lee

E-Mail Website
Guest Editor
Department of Biotechnology, Yonsei University, Seoul 03722, Republic of Korea
Interests: food biotechnology; microbiome; anaerobic microorganisms; directed evolution; enzyme engineering; multiomics
Prof. Dr. Moon-Suhn Ryu

E-Mail Website
Guest Editor
Department of Food and Nutrition, College of Human Ecology, Yonsei University, Seoul 03722, Republic of Korea
Interests: iron metabolism; ferritinophagy; zinc homeostasis; ZIP/ZnT transporters; nutritional genomics; anemia

Special Issue Information

Dear Colleagues,

Bioactive peptides (BPs) are referred to as organic substances formed by amino acids joined through covalent bonds such as amide or peptide bonds. BPs function as signal molecules contributing to cellular processes involved in physiology and metabolism. Numerous chemotherapeutic approaches for curing multifactorial diseases such as diabetes, cardiovascular diseases, neurodegenerative diseases, autoimmune diseases, and cancers have been introduced. However, chemical drugs, including synthetic peptides, showed several defects such as drug resistance, and toxic and off-target effects.

Natural BPs, encrypted in the food proteins and other natural sources, are released mainly by enzymatic hydrolysis and/or microbial fermentation during digestion in the gastrointestinal (GI) tract. Food-derived BPs have received significant attention due to their broad range of biological activities affecting digestive, immune, and nervous systems in the human gut against the predisposition of many metabolic diseases such as obesity and diabetes hypertension. Such a broad spectrum of biological activities highlights food-derived BPs as the next-generation food additives and/or therapeutic agents to prevent and treat various chronic diseases and disorders because they showed less toxic, highly specific, nonimmunogenic, and safe.

Despite the recent progress in the isolation and purification of BPs from several natural sources and the assessment of their bioactivities, BPs have limited usage in the market or at the commercial level due to technical barriers to overcome. Currently, new technologies are emerging to explore new food-derived BPs as food additives and functional ingredients, produce novel BPs using biocatalysts, and develop novel therapeutic agents contributing to improving human health. This special issue aims to augment, in detail, the recent findings and current ideas on the identification, bioassays, high-throughput screening, purification, production, and uses of BP in commercial products to identify/develop new BPs for promoting health benefits and/or curing human diseases. We welcome original research articles and reviews that cover areas including different physiological effects from BPs, the bioavailability of BPs after its intake, the methods of isolation of BPs from various protein sources with their in vitro and in vivo physiological effects, safety, and future application, but are not limited to:

  • Screening novel BPs using experimental and/or computational approaches
  • BPs discovery by enzyme-ligand interactions
  • Protein engineering for improving BPs’ activity and binding affinity
  • BPs as food additives and nutraceuticals
  • Therapeutic BPs
  • Prebiotic, probiotic, and postbiotic BPs

Prof. Dr. Dong-Woo Lee
Prof. Dr. Moon-Suhn Ryu
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • bioactive peptides
  • food additive
  • nutraceuticals
  • pharmaceuticals
  • postbiotics
  • biocatalysts
  • microbiome
  • fermentation

Published Papers (6 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

14 pages, 2362 KiB  
Article
Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera
by Xuejia Hu, Zhiyuan Dai and Renyao Jin
Foods 2022, 11(13), 1889; https://doi.org/10.3390/foods11131889 - 26 Jun 2022
Cited by 8 | Viewed by 1964
Abstract
In this study, Lepidotrigla microptera were hydrolyzed with four different proteolytic enzymes (Papain, neutrase, flavourzyme, and alcalase), and their distribution of molecular weights and ACE-inhibitory activity were tested. The alcalase hydrolysates showed the maximum ACE-inhibitory activity. A novel ACE-inhibitory peptide was isolated and [...] Read more.
In this study, Lepidotrigla microptera were hydrolyzed with four different proteolytic enzymes (Papain, neutrase, flavourzyme, and alcalase), and their distribution of molecular weights and ACE-inhibitory activity were tested. The alcalase hydrolysates showed the maximum ACE-inhibitory activity. A novel ACE-inhibitory peptide was isolated and purified from Lepidotrigla microptera protein hydrolysate (LMPH) using ultrafiltration, gel filtration chromatography, and preparative high performance liquid chromatography (prep-HPLC). The amino acid sequence of the purified peptide was identified as Phe-Leu-Thr-Ala-Gly-Leu-Leu-Asp (DLTAGLLE), and the IC50 value was 0.13 mg/mL. The ACE-inhibitory activity of DLTAGLLE was stable across a range of temperatures (<100 °C) and pH values (3.0–11.0) and retained after gastrointestinal digestion. DLTAGLLE was further identified as a noncompetitive inhibitor by Lineweaver–Burk plot. The molecular docking simulation showed that DLTAGLLE showed a high binding affinity with ACE sites by seven short hydrogen bonds. As the first reported antihypertensive peptide extracted from alcalase hydrolysate of Lepidotrigla microptera, DLTAGLLE has the potential to develop functional food or novel ACE-inhibitor drugs. Full article
(This article belongs to the Special Issue Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides)
►▼ Show Figures

Figure 1

12 pages, 1661 KiB  
Article
Prediction of ACE-I Inhibitory Peptides Derived from Chickpea (Cicer arietinum L.): In Silico Assessments Using Simulated Enzymatic Hydrolysis, Molecular Docking and ADMET Evaluation
by Jesús Gilberto Arámburo-Gálvez, Aldo Alejandro Arvizu-Flores, Feliznando Isidro Cárdenas-Torres, Francisco Cabrera-Chávez, Giovanni I. Ramírez-Torres, Lilian Karem Flores-Mendoza, Pedro Erick Gastelum-Acosta, Oscar Gerardo Figueroa-Salcido and Noé Ontiveros
Foods 2022, 11(11), 1576; https://doi.org/10.3390/foods11111576 - 27 May 2022
Cited by 20 | Viewed by 2740
Abstract
Chickpea (Cicer arietinum L.) peptides have shown in vitro potential to inhibit the angiotensin I-converting enzyme (ACE-I). However, the potential molecular interactions between chickpea peptides (CP) and ACE-I as well as their ADMET (absorption/distribution/metabolism/excretion/toxicity) characteristics remain unknown. Thus, our aim was to [...] Read more.
Chickpea (Cicer arietinum L.) peptides have shown in vitro potential to inhibit the angiotensin I-converting enzyme (ACE-I). However, the potential molecular interactions between chickpea peptides (CP) and ACE-I as well as their ADMET (absorption/distribution/metabolism/excretion/toxicity) characteristics remain unknown. Thus, our aim was to study the in silico interactions of CP with ACE-I and the CP ADMET characteristics. Legumin and provicilin sequences were submitted to in silico analysis to search for ACE-I inhibitory peptides. Simulated enzymatic hydrolysis was performed using the BIOPEP-UWM database, and the ACE-I inhibitory peptides generated (EC50 ≤ 200 μM) were selected to perform molecular docking and ADMET analysis. After hydrolysis, 59 out of 381 peptides with ACE-I inhibitory potential were released. Based on A and B parameters, the legumin peptides showed better ACE-I inhibitory potential than the provicilin ones. CP mainly interact with residues from pocket S1 (Ala354/Glu384) and S2 (His353/His513) through hydrogen bonds (distances < 3.0 Å) and hydrophobic interactions (binding energy from −5.7 to −9.2 kcal/mol). Through ADMET analysis, CP showed optimal values for inhibiting ACE-I in vivo. ACE-I inhibitory peptides from legumin and provicilin can bind strongly and tightly to the active site of ACE-I. Further studies to evaluate in vivo the antihypertensive effects of CP are warranted. Full article
(This article belongs to the Special Issue Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides)
►▼ Show Figures

Figure 1

19 pages, 3719 KiB  
Article
Using RSM for Optimum of Optimum Production of Peptides from Edible Bird’s Nest By-Product and Characterization of Its Antioxidant’s Properties
by Jie Cao, Ning Xiong, Yu Zhang, Yuwei Dai, Yuye Wang, Lingyu Lu and Lin Jiang
Foods 2022, 11(6), 859; https://doi.org/10.3390/foods11060859 - 18 Mar 2022
Cited by 9 | Viewed by 2168
Abstract
In this research, the neutrase hydrolysis conditions of edible bird’s nest (EBN) by-products were optimized by response surface methodology (RSM). Antioxidant peptides were then isolated from the EBN by-products by ultrafiltration and chromatography taking the DPPH radical scavenging ability as an indicator. The [...] Read more.
In this research, the neutrase hydrolysis conditions of edible bird’s nest (EBN) by-products were optimized by response surface methodology (RSM). Antioxidant peptides were then isolated from the EBN by-products by ultrafiltration and chromatography taking the DPPH radical scavenging ability as an indicator. The antioxidant activity of the purified peptides was estimated by radical scavenging ability and sodium nitroprusside (SNP)-induced damage model in PC12 cells. When the enzyme concentration was10 kU/g-hydrolysis temperature was 45 °C, and hydrolysis time was 10.30 h, the degree of hydrolysis (DH) of EBN by-product hydrolysate (EBNH) was the highest. The purified peptide exerted strong scavenging ability with EC50 values of 0.51, 1.31, and 0.65 mg/mL for DDPH, ABTS, and O2− radicals, respectively. In addition, the purified peptides could significantly reduce the SNP-induced oxidative damage of PC12 cells, and twelve peptides that were rich in leucine (Leu), valine (Val), and lysine (Lys) were identified by LC-MS/MS. These results suggested that EBN by-products have potential as new materials for natural antioxidant peptides. Full article
(This article belongs to the Special Issue Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides)
►▼ Show Figures

Figure 1

23 pages, 6180 KiB  
Article
Optimisation and Characterisation of Novel Angiotensin-Converting Enzyme Inhibitory Peptides Prepared by Double Enzymatic Hydrolysis from Agaricus bisporus Scraps
by Rui Wang, Jianmin Yun, Shujuan Wu, Yang Bi and Fengyun Zhao
Foods 2022, 11(3), 394; https://doi.org/10.3390/foods11030394 - 29 Jan 2022
Cited by 13 | Viewed by 2890
Abstract
Food-derived hypotensive peptides have attracted attention in the field of active peptide research in recent years. In this study, based on ACE inhibition rate and using the Box–Behnken central combination design principle to optimise the process of ACE inhibitor peptides prepared by double-enzyme [...] Read more.
Food-derived hypotensive peptides have attracted attention in the field of active peptide research in recent years. In this study, based on ACE inhibition rate and using the Box–Behnken central combination design principle to optimise the process of ACE inhibitor peptides prepared by double-enzyme hydrolysis. The amino acid sequences of ACE inhibitor peptides were determined by liquid chromatography mass spectrometry (LC-MS/MS), and their binding to ACE was studied by molecular docking. The optimal processing conditions were 1:1 alkaline protease: compound protease, pH was 8.43, enzymolysis temperature was 44.32 °C, and enzymolysis time was 3.52 h. Under these conditions, the ACE inhibition rate reached 65.12%, and the inhibition rate after separation and purification was 80.68% (IC50 = 0.9 mg/mL). Three novel peptides with ACE inhibitory activity were detected by LC-MS/MS, with sequences LVYP (Leu-Val-Tyr-Pro), VYPW(Val-Tyr-Pro-Trp) and YPWT(Tyr-Pro-Trp-Thr). Molecular docking revealed that the three novel peptides all established hydrogen bonds with the S1(Tyr523, Glu384, Ala354) and S2 (His353) pockets of ACE. Among them, LVYP, VYPW and YPWT, respectively, formed eleven hydrogen bonds, six hydrogen bonds and nine hydrogen bonds with ACE. The study revealed that these peptides have the potential for the development of novel ACE inhibitor drugs and provide a new avenue for high-value utilisation of mushrooms scraps. Full article
(This article belongs to the Special Issue Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides)
►▼ Show Figures

Figure 1

13 pages, 2106 KiB  
Article
In Silico Screening of a Bile Acid Micelle Disruption Peptide for Oral Consumptions from Edible Peptide Database
by Kento Imai, Yuri Takeuchi, Kazunori Shimizu and Hiroyuki Honda
Foods 2021, 10(10), 2496; https://doi.org/10.3390/foods10102496 - 18 Oct 2021
Cited by 3 | Viewed by 2558
Abstract
Recently, many bioactive peptides have been identified using bioinformatics tools. Previously, our group developed a method to screen dual-functional peptides that have direct intestinal delivery with porous silica gel and bile acid micelle disruption. However, newly designed peptides were not found in any [...] Read more.
Recently, many bioactive peptides have been identified using bioinformatics tools. Previously, our group developed a method to screen dual-functional peptides that have direct intestinal delivery with porous silica gel and bile acid micelle disruption. However, newly designed peptides were not found in any storage protein. Therefore, in this study, in silico screening was performed using a 350,000 edible peptide library consisting of 4- to 7-mer independent peptides. As an initial screening, all edible peptides were applied to the random forest model to select predicted positive peptides. For a second screening, the peptides were assessed for the possibility of intestinal delivery using a 3D color map. From this approach, three novel dual-functional peptides, VYVFDE, WEFIDF, and VEEFYC were identified, and all of them were derived from storage proteins (legumin, myosin, and 11S globulin). In particular, VEEFYCS, in which a serine residue (S) is added to VEEFYC, was assumed to be released by thermolysin from the 11S-globulin derived from Ginkgo biloba by LC-MS/MS analysis. VEEFYCS was found to have suitable direct intestinal delivery and bile acid micelle disruption activity. Full article
(This article belongs to the Special Issue Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides)
►▼ Show Figures

Figure 1

11 pages, 1249 KiB  
Article
Partial-, Double-Enzymatic Dephosphorylation and EndoGluC Hydrolysis as an Original Approach to Enhancing Identification of Casein Phosphopeptides (CPPs) by Mass Spectrometry
by Barbara Deracinois, Aurélie Matéos, Audrey Romelard, Audrey Boulier, Julie Auger, Alain Baniel, Rozenn Ravallec and Christophe Flahaut
Foods 2021, 10(9), 2134; https://doi.org/10.3390/foods10092134 - 09 Sep 2021
Cited by 5 | Viewed by 1877
Abstract
The identification of phosphopeptides is currently a challenge when they are part of a complex matrix of peptides, such as a milk protein enzymatic hydrolysate. This challenge increases with both the number of phosphorylation sites on the phosphopeptides and their amino acid length. [...] Read more.
The identification of phosphopeptides is currently a challenge when they are part of a complex matrix of peptides, such as a milk protein enzymatic hydrolysate. This challenge increases with both the number of phosphorylation sites on the phosphopeptides and their amino acid length. Here, this paper reports a four-phase strategy from an enzymatic casein hydrolysate before a mass spectrometry analysis in order to enhance the identification of phosphopeptides and phosphosites: (i) the control protein hydrolysate, (ii) a two-step enzymatic dephosphorylation of the latter, allowing for the almost total dephosphorylation of peptides, (iii) a one-step enzymatic dephosphorylation, allowing for the partial dephosphorylation of the peptides and (iv) an additional endoGluC enzymatic hydrolysis, allowing for the cleavage of long-size peptides into shorter ones. The reverse-phase high-pressure liquid chromatography–tandem mass spectrometry (RP-HPLC-MS/MS) analyses of hydrolysates that underwent this four-phase strategy allowed for the identification of 28 phosphorylation sites (90%) out of the 31 referenced in UniprotKB/Swiss-Prot (1 June 2021), compared to 17 sites (54%) without the latter. The alpha-S2 casein phosphosites, referenced by their similarity in the UniProt database, were experimentally identified, whereas pSer148, pThr166 and pSer187 from a multiphosphorylated long-size kappa-casein were not. Data are available via ProteomeXchange with identifier PXD027132. Full article
(This article belongs to the Special Issue Current State-of-the-Art Technologies for Exploring Food-Derived Bioactive Peptides)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-6
Back to TopTop