Special Issue "Research of Bioactive Peptides in Foods"

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Food Science and Technology".

Deadline for manuscript submissions: 30 November 2020.

Special Issue Editor

Prof. Dr. Piotr Minkiewicz
Website SciProfiles
Guest Editor
Chair of Food Biochemistry, University of Warmia and Mazury in Olsztyn, Plac Cieszyński 1, 10-726 Olsztyn-Kortowo, Poland
Interests: protein and peptide analysis with the HPLC, MS, 2D-PAGE methods; proteomics; peptidomics of food, bioinformatics and chemical information

Special Issue Information

Dear Colleagues,

In recent years, peptides have received increased interest as one of the most important classes of bioactive food components. They are important as nutraceutical and active components in foods designed to obtain health benefits above and beyond their nutritional function. Peptides sufficient in diet aimed on metabolic syndrome prevention may serve as an example of compounds providing such benefits. Contemporary research includes, e.g., the discovery of novel bioactive peptides in food products and new activities of known compounds. The design and optimization of technological processes aimed at peptide release is an important task for food science and technology. The development of research strategies (e.g., in vitro and in vivo assays as well as bioinformatics) and analytical methods for identification and quantitation of biopeptides is also receiving major attention. Taste is one of the crucial factors affecting the acceptance of peptide-containing food products by consumers.

This Special Issue, entitled “Research of Bioactive Peptides in Foods”, will cover a selection of recent research articles, short communications, reviews, as well as perspectives in the area of bioactive peptides of food origin.

Prof. Dr. Piotr Minkiewicz
Guest Editor

Manuscript Submission Information

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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. Applied Sciences 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 1800 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 of food origin
  • in vivo, in vitro, and in silico studies
  • peptide identification and determination
  • release of peptides during food processing
  • taste of peptides

Published Papers (4 papers)

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Research

Open AccessFeature PaperArticle
Characterisation of Seasonal Mytilus edulis By-Products and Generation of Bioactive Hydrolysates
Appl. Sci. 2020, 10(19), 6892; https://doi.org/10.3390/app10196892 - 01 Oct 2020
Abstract
Mussel cultivation results in tons of by-product, with 27% of the harvest considered as reject material. In this study, mussel by-products considered to be undersized (mussels with a cooked meat yield <30%), mussels with broken shells and barnacle-fouled mussels were collected from three [...] Read more.
Mussel cultivation results in tons of by-product, with 27% of the harvest considered as reject material. In this study, mussel by-products considered to be undersized (mussels with a cooked meat yield <30%), mussels with broken shells and barnacle-fouled mussels were collected from three different locations in the west, north-west and south-west of Ireland. Samples were hydrolysed using controlled temperatures and agitation, and the proteolytic enzyme Protamex® was added at an enzyme:substrate ratio of 1:50 (w:v). The hydrolysates were freeze-dried and analysed for protein content and amino acid composition, lipid content and fatty acid methyl ester (FAME) composition, ash and techno-functional and bioactive activities. The degree of hydrolysis was determined using the Adler-Nissen pH stat method and was found to be between 2.41% ± 0% and 7.55% ± 0.6%. Mussel by-products harvested between February and May 2019 had protein contents ranging from 36.76% ± 0.41% to 52.19% ± 1.78%. The protein content of mussels collected from July to October (the spawning season) ranged from 59.07% ± 1.375% to 68.31% ± 3.42%. The ratio of essential to nonessential amino acids varied from 0.68–0.96 and it was highest for a sample collected in November from the west of Ireland. All the hydrolysate samples contained omega-3 polyunsaturated fatty acids (PUFA), especially eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), which are known anti-inflammatory agents. Selected hydrolysates which had angiotensin-converting enzyme I (ACE-I; EC 3.4.15.1) and dipeptidyl peptidase IV (DPP-IV; EC 3.4.14.5) inhibitory activities were filtered using 3-kDa membrane filtration and the permeate fraction was sequenced using mass spectrometry (MS). Identified peptides were >7 amino acids in length. Following BIOPEP database mining, 91% of the by-product mussel peptides identified were found to be previously identified DPP-IV and ACE-I inhibitory peptides, and this was confirmed using in vitro bioassays. The ACE-I inhibitory activity of the by-product mussel hydrolysates ranged from 22.23% ± 1.79% to 86.08% ± 1.59% and the most active hydrolysate had an ACE-I inhibitory concentration (IC50) value of 0.2944 mg/mL compared to the positive control, captopril. This work demonstrates that by-product mussel hydrolysates have potential for use as health-promoting ingredients. Full article
(This article belongs to the Special Issue Research of Bioactive Peptides in Foods)
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Open AccessArticle
Antihypertensive Effect of Amaranth Hydrolysate Is Comparable to the Effect of Low-Intensity Physical Activity
Appl. Sci. 2020, 10(16), 5706; https://doi.org/10.3390/app10165706 - 17 Aug 2020
Abstract
Background and objectives: Both antihypertensive peptide intake and physical activity help to control blood pressure. Our aim was to evaluate the impact of consuming amaranth antihypertensive peptides on systolic blood pressure (SBP) in normotensive rats and the magnitude and relevance of the peptide-induced [...] Read more.
Background and objectives: Both antihypertensive peptide intake and physical activity help to control blood pressure. Our aim was to evaluate the impact of consuming amaranth antihypertensive peptides on systolic blood pressure (SBP) in normotensive rats and the magnitude and relevance of the peptide-induced antihypertensive effect in spontaneously hypertensive rats (SHR). Materials and Methods: Treatments (alcalase-generated amaranth protein hydrolysate, captopril, or water) were given by gavage and the SBP measured by the tail-cuff method. Physical activity was performed five days/week (for twenty weeks). Results: The normotensive rats’ SBP (mmHg, average/group) remained unaffected after amaranth antihypertensive peptide supplementation (121.8) (p > 0.05 vs controls). In SHR, the SBP was lowered by 24.6 (sedentary/supplemented at two weeks), 42.0 (sedentary/supplemented at eight weeks), and 31.5 (exercised/non-supplemented at eight weeks) (p < 0.05 vs sedentary/non-supplemented). The combination of supplementation and physical activity lowered the SBP by 36.2 and 42.7 (supplemented/exercised at two weeks and eight weeks, respectively) (p < 0.05 vs sedentary/non-supplemented), but it did not have additional antihypertensive benefits (p > 0.05 vs sedentary/supplemented at eight weeks or exercised/non-supplemented at eight weeks). Conclusions: Amaranth antihypertensive peptide supplementation has no impact on SBP in normotensive rats. This supplementation develops sustained antihypertensive benefits in SHR, which are similar to the antihypertensive effect developed after eight- or twenty-week low-intensity physical activity. These findings have implications for developing safe and effective peptide-based functional foods. Full article
(This article belongs to the Special Issue Research of Bioactive Peptides in Foods)
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Open AccessArticle
Effect of Molecular Weight of Tilapia (Oreochromis Niloticus) Skin Collagen Peptide Fractions on Zinc-Chelating Capacity and Bioaccessibility of the Zinc-Peptide Fractions Complexes in Vitro Digestion
Appl. Sci. 2020, 10(6), 2041; https://doi.org/10.3390/app10062041 - 17 Mar 2020
Abstract
To investigate the effect of the molecular weight of tilapia skin collagen peptide fractions on their zinc chelation capacity and the bioaccessibility of their zinc complexes, we evaluated the zinc-chelating ability of different molecular weight peptide, the solubility, and the stability of the [...] Read more.
To investigate the effect of the molecular weight of tilapia skin collagen peptide fractions on their zinc chelation capacity and the bioaccessibility of their zinc complexes, we evaluated the zinc-chelating ability of different molecular weight peptide, the solubility, and the stability of the complexes during simulated in vitro digestion. Low molecular weight peptide (P1) exhibited a higher zinc-chelating ability, which can be attributed to the variety of metal chelate amino acid residues. The highest solubility and the lowest release of zinc during peptic digestion for the P1-zinc complex and the zinc binding to P1 were retained at approximately 50% after peptic-pancreatic digestion. Fourier transform infrared spectroscopy indicated the primary involvement of the N-H group in all peptide-zinc complexes. This finding suggests that low molecular weight peptidefraction with strong zinc chelation ability can be used as delivery agents to improve zinc bioaccessibility. Full article
(This article belongs to the Special Issue Research of Bioactive Peptides in Foods)
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Open AccessArticle
Hypolipidemic Activities of Two Pentapeptides (VIAPW and IRWWW) from Miiuy Croaker (Miichthys miiuy) Muscle on Lipid Accumulation in HepG2 Cells through Regulation of AMPK Pathway
Appl. Sci. 2020, 10(3), 817; https://doi.org/10.3390/app10030817 - 23 Jan 2020
Abstract
In this work, the hypolipidemic activities of two pentapeptides (VIAPW and IRWWW) from miiuy croaker (Miichthys miiuy) muscle on oleic acid (OA)-induced lipid accumulation in HepG2 cells were investigated. VIAPW and IRWWW could significantly inhibit lipid accumulation induced by OA and [...] Read more.
In this work, the hypolipidemic activities of two pentapeptides (VIAPW and IRWWW) from miiuy croaker (Miichthys miiuy) muscle on oleic acid (OA)-induced lipid accumulation in HepG2 cells were investigated. VIAPW and IRWWW could significantly inhibit lipid accumulation induced by OA and decreased intracellular levels of intracellular triglyceride (TG) and total cholesterol (TC) in a dose-effect dependence manner. At the concentration of 100 μm, the TG levels of VIAPW (0.201 ± 0.006 mm) and IRWWW (0.186 ± 0.005 mm) were very (p < 0.01) and extremely (p < 0.001) significantly lower than those (0.247 ± 0.004 mm) of the OA model group; the levels of TC of VIAPW (45.88 ± 0.74 μg/mg protein) and IRWWW (41.02 ± 0.14 μg/mg protein) were very (p < 0.01) and extremely (p < 0.001) significantly lower than that (53.45 ± 0.10μg/mg protein) of the OA model group (p < 0.01). The hypolipidemic mechanisms of VIAPW and IRWWW were to down-regulate the expression levels of genes of SREBP-1c, SREBP-2, FAS, ACC, and HMGR in lipid synthesis and to up-regulate the expression levels of genes of PPARα, ACOX-1, and CPT-1 in lipid oxidation. These results suggested that VIAPW and IRWWW could play their hypolipidemic activities in HepG2 cells through regulation of AMPK pathway and act as hypolipidemic nutrient ingredients applied in public healthy and functional foods. Full article
(This article belongs to the Special Issue Research of Bioactive Peptides in Foods)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Molecular Docking Analysis of Human Somatic and Testicular Angiotensin Converting Enzyme in Complexed with a Novel Tripeptide Gly-Val-Arg

Author:Sivananthan Manoharan

Abstract: The structure-based drug design targeting domains of the angiotensin-I-converting enzyme (ACE) is important in the treatment of hypertension. The domain specificity inhibition of somatic and testicular ACE by tripeptide GVR isolated from grey oyster mushroom by binding to the specified active site of ACE was not described previously. Tripeptide GVR was used as a ligand while different types of ACE proteins were used as receptors. Molecular docking studies were carried out. Tripeptide GVR was significantly bound to the active site of C-domain of somatic ACE as compared to the N-domain. Although tripeptide GVR was mimicking captopril but a strong inhibition of C-domain and a weak inhibition of N-domain by GVR probably lead to the less significant side effects to the patients as compared to the strong non-domain specific inhibitor, captopril. Besides, the importance of arginine at the C-terminal of a peptide sequence to inhibit ACE significantly was also shown.

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