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

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 29034

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Prof. Dr. Piotr Minkiewicz

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Department of Food Biochemistry, Faculty of Food Science, University of Warmia and Mazury in Olsztyn, 10-726 Olsztyn, Kortowo, Poland
Interests: food proteins; mass spectrometry; chromatography; bioinformatics
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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

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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

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Published Papers (6 papers)

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Research

Jump to: Review

13 pages, 1414 KiB

Open AccessArticle

Isolation, Purification and Characterization of Proteins in “Señorita” Banana (Musa acuminata (AAA) ‘Señorita’) Pulp with Bioactive Peptides Exhibiting Antihypertensive and Antioxidant Activities

by John Matthew Ferreras, Mia Claire Marie Clemencia, Amelia Hizon-Fradejas, Lawrence Yves Uy and Mary Ann Torio

Appl. Sci. 2021, 11(5), 2190; https://doi.org/10.3390/app11052190 - 3 Mar 2021

Cited by 8 | Viewed by 5424

Abstract

Banana is one of the most important crops, providing multiple benefits. Although it has been widely studied for its health benefits, little information can be found about its proteins. This study determined the antihypertensive and antioxidant activities of the crude, purified, and hydrolyzed protein extracts from ‘Señorita’ banana pulp. Crude proteins were extracted using Tris-HCl buffer and purified through ammonium sulfate precipitation, dialysis, and gel filtration chromatography. The protein content of the crude, partially purified, and purified extracts were found to be 167.32, 120.45, and 28.51 μg·mL⁻¹, respectively, with major protein having an approximate molecular weight of 15 kDa. These extracts were then subjected to enzymatic hydrolysis for release of bioactive peptides prior to ACE inhibitory and antioxidant activities determination. Among these samples, the undigested crude extract had the highest ACE inhibitory activity (85.20%). There was also an observable increase in ACE inhibition of the digested samples with increased digestion time. Meanwhile, the 3-h and 4-h crude digests had the highest DPPH radical scavenging activity with 30.82% and 34.74%, respectively. These were not significantly different from the activity of the standard, ascorbic acid. A general decrease in DPPH radical scavenging activity of the samples was observed with increased digestion time. These observations were coherent with the in silico analysis of the putative major protein, lectin, which showed that its enzymatic hydrolysis releases ACE inhibitor and antioxidant peptides. Full article

(This article belongs to the Special Issue Research of Bioactive Peptides in Foods)

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21 pages, 7012 KiB

Open AccessFeature PaperArticle

Characterisation of Seasonal Mytilus edulis By-Products and Generation of Bioactive Hydrolysates

by Azza Silotry Naik, Leticia Mora and Maria Hayes

Appl. Sci. 2020, 10(19), 6892; https://doi.org/10.3390/app10196892 - 1 Oct 2020

Cited by 14 | Viewed by 3403

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 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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10 pages, 1588 KiB

Open AccessArticle

Antihypertensive Effect of Amaranth Hydrolysate Is Comparable to the Effect of Low-Intensity Physical Activity

by Francisco Cabrera-Chávez, Veronica Lopez-Teros, Perla Yareli Gutiérrez-Arzapalo, Feliznando Isidro Cárdenas-Torres, Efren Rafael Rios-Burgueño, Humberto Astiazaran-Garcia, José Aldo Hernández Murúa, Guadalupe González-Ochoa, Giovanni Isaí Ramírez-Torres and Noé Ontiveros

Appl. Sci. 2020, 10(16), 5706; https://doi.org/10.3390/app10165706 - 17 Aug 2020

Cited by 5 | Viewed by 3207

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 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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11 pages, 830 KiB

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

by Lei Chen, Xuanri Shen and Guanghua Xia

Appl. Sci. 2020, 10(6), 2041; https://doi.org/10.3390/app10062041 - 17 Mar 2020

Cited by 25 | Viewed by 3423

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 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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13 pages, 2445 KiB

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

by Yu-Mei Wang, Xin Pan, Yu He, Chang-Feng Chi and Bin Wang

Appl. Sci. 2020, 10(3), 817; https://doi.org/10.3390/app10030817 - 23 Jan 2020

Cited by 21 | Viewed by 2734

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 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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Review

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39 pages, 3313 KiB

Open AccessReview

Legumes as Functional Food for Cardiovascular Disease

by Jorge Gil C. Angeles, Jeric C. Villanueva, Lawrence Yves C. Uy, Sheila Mae Q. Mercado, Maria Claret L. Tsuchiya, Jickerson P. Lado, Mark Rickard N. Angelia, Mia Clare Marie Bercansil-Clemencia, Maria Amelita C. Estacio and Mary Ann O. Torio

Appl. Sci. 2021, 11(12), 5475; https://doi.org/10.3390/app11125475 - 12 Jun 2021

Cited by 21 | Viewed by 9876

Abstract

Legumes are an essential food source worldwide. Their high-quality proteins, complex carbohydrates, dietary fiber, and relatively low-fat content make these an important functional food. Known to possess a multitude of health benefits, legume consumption is associated with the prevention and treatment of cardiovascular diseases (CVD). Legume crude protein isolates and purified peptides possess many cardiopreventive properties. Here, we review selected economically valued legumes, their taxonomy and distribution, biochemical composition, and their protein components and the mechanism(s) of action associated with cardiovascular health. Most of the legume protein studies had shown upregulation of low-density lipoprotein (LDL) receptor leading to increased binding and uptake, in effect significantly reducing total lipid levels in the blood serum and liver. This is followed by decreased biosynthesis of cholesterol and fatty acids. To understand the relationship of identified genes from legume studies, we performed gene network analysis, pathway, and gene ontology (GO) enrichment. Results showed that the genes were functionally interrelated while enrichment and pathway analysis revealed involvement in lipid transport, fatty acid and triglyceride metabolic processes, and regulatory processes. This review is the first attempt to collate all known mechanisms of action of legume proteins associated with cardiovascular health. This also provides a snapshot of possible targets leading to systems-level approaches to further investigate the cardiometabolic potentials of legumes. Full article

(This article belongs to the Special Issue Research of Bioactive Peptides in Foods)

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