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Bioactive Peptides: Characteristic, Bioavailability and Application
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Bioactive Peptides: Characteristic, Bioavailability and Application

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Nutraceuticals, Functional Foods, and Novel Foods".

Deadline for manuscript submissions: closed (20 June 2021) | Viewed by 41024

Special Issue Editors

Dr. Anna Jakubczyk

E-Mail Website
Guest Editor
Department of Biochemistry and Food Chemistry, The University of Life Sciences, Skromna 8 St., 20-704 Lublin, Poland
Interests: biochemistry; food chemistry; bioactive compounds; plant; health; nutrition
Special Issues, Collections and Topics in MDPI journals
Dr. Monika Karaś

E-Mail Website
Guest Editor
Department of Biochemistry and Food Chemistry, Faculty of Food Sciences and Biotechnology, University of Life Sciences in Lublin, 20-704 Lublin, Poland
Interests: food science; food bioactive compounds; antioxidant activity; bioactive peptides; protein hydrolysates; functional food; food fortification; functional properties of proteins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In recent years, food has become the subject of research as a source of not only essential nutrients required for proper functioning of the organism, but also bioactive compounds. These include bioactive peptides, which may be present in foodstuffs as free compounds and released during the digestion of food or as a result of technological processes, especially in protein-rich products. They may have health-promoting properties, such as antioxidant, antihypertensive, anti-obesity, or anti-inflammatory properties. Moreover, they may have technological application by improving functional properties (water-holding capacity, foaming capacity, emulsifying properties, or solubility) and giving flavor or aroma.

Biologically active peptides can be obtained from various sources of protein. It is important to choose those from which, also after a targeted technological treatment, peptides with specific physiological effects will be released through proteolytic hydrolysis and enter the bloodstream. Determination of the composition and bioavailability of amino acids can provide new knowledge about the relationship between the structure and activity of peptides. Bioactive peptides isolated and identified from food protein sources can therefore be used in the design of foodstuffs intended for particular nutritional or dietary purposes.

Dr. Anna Jakubczyk
Dr. Monika Karaś
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

  • peptides
  • proteins
  • hydrolysis
  • bioavailability
  • biological activity
  • food technology
  • functional properties

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Published Papers (7 papers)

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Research

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12 pages, 1564 KiB  
Article
Production of ACE Inhibitory Peptides from Whey Proteins Modified by High Intensity Ultrasound Using Bromelain
by Lucía Abadía-García, Eduardo Castaño-Tostado, Anaberta Cardador-Martínez, Sandra Teresita Martín-del-Campo and Silvia L. Amaya-Llano
Foods 2021, 10(9), 2099; https://doi.org/10.3390/foods10092099 - 5 Sep 2021
Cited by 13 | Viewed by 3077
Abstract
High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at [...] Read more.
High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at two levels of amplitude (30 and 50%) for 10 min, followed by hydrolysis using the vegetable protease bromelain. The hydrolysates obtained were ultrafiltrated and their fractions were submitted to a simulated gastrointestinal digestion. The conformational changes induced by HIUS on whey proteins were analyzed using Fourier-transform infrared spectroscopy by attenuated total reflectance (FTIR-ATR) and intrinsic spectroscopy. It was found that both levels of ultrasound pretreatment significantly decreased the IC50 value (50% Inhibitory Concentration) of the hydrolysates in comparison with the control (α = 0.05). After this treatment, HIUS-treated fractions were shown as smaller in size and fractions between 1 and 3 kDa displayed the highest ACE inhibition activity. HIUS promoted significant changes in whey protein structure, inducing, unfolding, and aggregation, decreasing the content of α-helix, and increasing β-sheets structures. These findings prove that ultrasound treatment before enzymatic hydrolysis is an innovative and useful strategy that modifies the peptide profile of whey protein hydrolysates and enhances the production of ACE inhibitory peptides. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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19 pages, 2925 KiB  
Article
Partial Purification and Characterization of Bioactive Peptides from Cooked New Zealand Green-Lipped Mussel (Perna canaliculus) Protein Hydrolyzates
by Ramya Jayaprakash and Conrad O. Perera
Foods 2020, 9(7), 879; https://doi.org/10.3390/foods9070879 - 4 Jul 2020
Cited by 24 | Viewed by 4362
Abstract
Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, [...] Read more.
Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, named GPH, exhibited the highest antioxidant and ACE inhibitory activity, but no antimicrobial activity. Purification of the GPH using gel-filtration chromatography revealed that the protein fraction (GPH-IV*) containing peptides with a molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities. Further purification was done using reverse-phase HPLC (RP-HPLC) and the only major peak obtained (GPH-IV*-P2) had the highest antioxidant and ACE inhibitory activity. From this fraction, several bioactive peptides with an MW ≈ 5 kDa were identified using LC-MS and in silico analyses. This research highlights that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with potential therapeutic applications. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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18 pages, 892 KiB  
Article
Characterisation of Biologically Active Hydrolysates and Peptide Fractions of Vacuum Packaging String Bean (Phaseolus Vulgaris L.)
by Anna Jakubczyk, Monika Karaś, Piotr Stanikowski, Beata Rutkowska, Magdalena Dziedzic, Ewelina Zielińska, Konrad A. Szychowski, Urszula E. Binduga, Kamila Rybczyńska-Tkaczyk and Barbara Baraniak
Foods 2020, 9(7), 842; https://doi.org/10.3390/foods9070842 - 28 Jun 2020
Cited by 9 | Viewed by 3373
Abstract
The aim of the study is to characterise biologically active hydolysates and peptide fractions obtained from vacuum-packed string beans (Phaseolus vulragis L.) (PB). Unpacked beans were a control sample. The influence on human squamous carcinoma cell line SCC-15 (ATCC CRL-1623) was determined. [...] Read more.
The aim of the study is to characterise biologically active hydolysates and peptide fractions obtained from vacuum-packed string beans (Phaseolus vulragis L.) (PB). Unpacked beans were a control sample. The influence on human squamous carcinoma cell line SCC-15 (ATCC CRL-1623) was determined. Packed bean (PB) and unpacked bean (UB) extracts were found to exert no effect on the tongue squamous carcinoma cells. The results of the study indicated that the packing process contributed to the retention of protein, soluble dietary fibre, and free sugar (2.36, 3.5, and 1.79 g/100 d.m., respectively). PB was characterised by higher antioxidant activity (expressed as neutralisation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS ABTS•+) and 2,2-diphenyl-1-picrylhydrazyl (DPPH·) free radicals) as well as Fe2+ chelation and reducing power (IC50 = 54.56, 0.46, 3.85 mg mL−1; 0.088 A700/peptide content, respectively) than the UB samples before hydrolysis. The hydrolysis process enhanced these properties. The IC50 value of lipase and α-amylase inhibitory activity of the hydrolysates obtained from UB was reduced. The PB and UB fractions exhibited a certain level of antimicrobial activity against S. aureus and E. coli. Candida albicans were not sensitive to these peptide fractions. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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11 pages, 1918 KiB  
Article
Purification of Bioactive Peptide with Antimicrobial Properties Produced by Saccharomyces cerevisiae
by Shayma Thyab Gddoa Al-sahlany, Ammar B. Altemimi, Alaa Jabbar Abd Al-Manhel, Alaa Kareem Niamah, Naoufal Lakhssassi and Salam A. Ibrahim
Foods 2020, 9(3), 324; https://doi.org/10.3390/foods9030324 - 11 Mar 2020
Cited by 56 | Viewed by 6466
Abstract
A variety of organisms produce bioactive peptides that express inhibition activity against other organisms. Saccharomyces cerevisiae is considered the best example of a unicellular organism that is useful for studying peptide production. In this study, an antibacterial peptide was produced and isolated from [...] Read more.
A variety of organisms produce bioactive peptides that express inhibition activity against other organisms. Saccharomyces cerevisiae is considered the best example of a unicellular organism that is useful for studying peptide production. In this study, an antibacterial peptide was produced and isolated from Saccharomyces cerevisiae (Baker’s yeast) by an ultrafiltration process (two membranes with cut-offs of 2 and 10 kDa) and purified using the ÄKTA Pure 25 system. Antibacterial peptide activity was characterized and examined against four bacterial strains including Gram-positive and Gram-negative bacteria. The optimum condition for yeast growth and antibacterial peptide production against both Escherichia. coli and Klebsiella aerogenes was 25–30 °C within a 48 h period. The isolated peptide had a molecular weight of 9770 Da, was thermostable at 50–90 °C for 30 min, and tolerated a pH range of 5–7 at 4 °C and 25 °C during the first 24 h, making this isolated antibacterial peptides suitable for use in sterilization and thermal processes, which are very important aspect in food production. The isolated antibacterial peptide caused a rapid and steady decline in the number of viable cells from 2 to 2.3 log units of gram-negative strains and from 1.5 to 1.8 log units of gram-positive strains during 24 h of incubation. The isolated antibacterial peptide from Saccharomyces cerevisiae may present a potential biopreservative compound in the food industry exhibiting inhibition activity against gram-negative and gram-positive bacteria. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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10 pages, 951 KiB  
Article
Pasta Enrichment with an Amaranth Hydrolysate Affects the Overall Acceptability while Maintaining Antihypertensive Properties
by Eduardo Enrique Valdez-Meza, Anabela Raymundo, Oscar Gerardo Figueroa-Salcido, Giovanni Isaí Ramírez-Torres, Patrícia Fradinho, Sonia Oliveira, Isabel de Sousa, Miroslava Suárez-Jiménez, Feliznando Isidro Cárdenas-Torres, Alma Rosa Islas-Rubio, Guillermo Rodríguez-Olibarría, Noé Ontiveros and Francisco Cabrera-Chávez
Foods 2019, 8(8), 282; https://doi.org/10.3390/foods8080282 - 24 Jul 2019
Cited by 21 | Viewed by 4115
Abstract
Background: Alcalase-treated amaranth proteins generate angiotensin-1-converting enzyme (ACE-1) inhibitory peptides, which could be useful for functional foods development. Our aim was to evaluate the technological, sensory, and antihypertensive properties of pasta enriched with an amaranth hydrolysate. Methods: Pasta with 11% (A; control), 15% [...] Read more.
Background: Alcalase-treated amaranth proteins generate angiotensin-1-converting enzyme (ACE-1) inhibitory peptides, which could be useful for functional foods development. Our aim was to evaluate the technological, sensory, and antihypertensive properties of pasta enriched with an amaranth hydrolysate. Methods: Pasta with 11% (A; control), 15% (B), and 20% (C) of protein content were formulated. Pastas B and C were supplemented with an alcalase-treated amaranth protein concentrate. Cooking time, cooking lost, color, and texture were assessed. An untrained panel (n = 30) evaluated sensory attributes. The antihypertensive effect was evaluated in hypertensive rats. Results: The hydrolysate IC50 was 0.014 mg/mL. Optimum cooking time and cooking loss decreased in products B and C vs. A (p < 0.05). The L* values decreased in pasta C. Firmness increased in pasta C vs. A (p < 0.05). Adhesiveness was different among groups (p < 0.05). Pasta A had the highest acceptability (p < 0.05). The products B and C, and captopril (positive control) showed antihypertensive properties after 3 h of supplementation (p < 0.05). This effect remained after 7 h, 8 h, or 9 h. Conclusions: The addition of amaranth hydrolysates to pasta negatively impacts on the overall acceptability and, to a lesser extent, on pasta taste. However, it is possible to maintain the antihypertensive properties of the supplemented pasta under physiological conditions. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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Review

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34 pages, 938 KiB  
Review
Antidiabetic Food-Derived Peptides for Functional Feeding: Production, Functionality and In Vivo Evidences
by Fernando Rivero-Pino, F. Javier Espejo-Carpio and Emilia M. Guadix
Foods 2020, 9(8), 983; https://doi.org/10.3390/foods9080983 - 23 Jul 2020
Cited by 66 | Viewed by 8252
Abstract
Bioactive peptides released from the enzymatic hydrolysis of food proteins are currently a trending topic in the scientific community. Their potential as antidiabetic agents, by regulating the glycemic index, and thus to be employed in food formulation, is one of the most important [...] Read more.
Bioactive peptides released from the enzymatic hydrolysis of food proteins are currently a trending topic in the scientific community. Their potential as antidiabetic agents, by regulating the glycemic index, and thus to be employed in food formulation, is one of the most important functions of these peptides. In this review, we aimed to summarize the whole process that must be considered when talking about including these molecules as a bioactive ingredient. In this regard, at first, the production, purification and identification of bioactive peptides is summed up. The detailed metabolic pathways described included carbohydrate hydrolases (glucosidase and amylase) and dipeptidyl-peptidase IV inhibition, due to their importance in the food-derived peptides research field. Then, their characterization, concerning bioavailability in vitro and in situ, stability and functionality in food matrices, and ultimately, the in vivo evidence (from invertebrate animals to humans), was described. The future applicability that these molecules have due to their biological potential as functional ingredients makes them an important field of research, which could help the world population avoid suffering from several diseases, such as diabetes. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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28 pages, 1090 KiB  
Review
Current Trends of Bioactive Peptides—New Sources and Therapeutic Effect
by Anna Jakubczyk, Monika Karaś, Kamila Rybczyńska-Tkaczyk, Ewelina Zielińska and Damian Zieliński
Foods 2020, 9(7), 846; https://doi.org/10.3390/foods9070846 - 29 Jun 2020
Cited by 148 | Viewed by 10204
Abstract
Generally, bioactive peptides are natural compounds of food or part of protein that are inactive in the precursor molecule. However, they may be active after hydrolysis and can be transported to the active site. Biologically active peptides can also be synthesized chemically and [...] Read more.
Generally, bioactive peptides are natural compounds of food or part of protein that are inactive in the precursor molecule. However, they may be active after hydrolysis and can be transported to the active site. Biologically active peptides can also be synthesized chemically and characterized. Peptides have many properties, including antihypertensive, antioxidant, antimicrobial, anticoagulant, and chelating effects. They are also responsible for the taste of food or for the inhibition of enzymes involved in the development of diseases. The scientific literature has described many peptides with bioactive properties obtained from different sources. Information about the structure, origin, and properties of peptides can also be found in many databases. This review will describe peptides inhibiting the development of current diseases, peptides with antimicrobial properties, and new alternative sources of peptides based on the current knowledge and documentation of their bioactivity. All these issues are part of modern research on peptides and their use in current health or technological problems in food production. Full article
(This article belongs to the Special Issue Bioactive Peptides: Characteristic, Bioavailability and Application)
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