Foods

Editorial

Jump to: Research

3 pages, 180 KiB

Open AccessEditorial

Proteins and Bioactive Peptides in High Protein Content Foods

by Fidel Toldrá and Leticia Mora

Foods 2021, 10(6), 1186; https://doi.org/10.3390/foods10061186 - 25 May 2021

Cited by 1 | Viewed by 1837

Abstract

Foods and their industry by-products constitute very good sources of bioactive peptides, which can be naturally generated during processing but are also extensively produced through enzymatic hydrolysis, microbial fermentation, and even during gastrointestinal digestion in the human body [...] Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

Research

Jump to: Editorial

9 pages, 941 KiB

Open AccessCommunication

Alternative Proteins as a Source of Bioactive Peptides: The Edible Snail and Generation of Hydrolysates Containing Peptides with Bioactive Potential for Use as Functional Foods

by Maria Hayes and Leticia Mora

Foods 2021, 10(2), 276; https://doi.org/10.3390/foods10020276 - 30 Jan 2021

Cited by 5 | Viewed by 2907

Abstract

Members of the Phylum Mollusca include shellfish such as oysters and squid but also the edible garden snail known as Helix aspersa. This snail species is consumed as a delicacy in countries including France (where they are known as petit-gris), southern Spain [...] Read more.

Members of the Phylum Mollusca include shellfish such as oysters and squid but also the edible garden snail known as Helix aspersa. This snail species is consumed as a delicacy in countries including France (where they are known as petit-gris), southern Spain (where they are known as Bobe), Nigeria, Greece, Portugal and Italy but is not a traditional food in many other countries. However, it is considered an excellent protein source with a balanced amino acid profile and an environmentally friendly, sustainable protein source. The aim of this work was to develop a different dietary form of snail protein by generating protein hydrolysate ingredients from the edible snail using enzyme technology. A second aim was to assess the bioactive peptide content and potential health benefits of these hydrolysates. H. aspersa hydrolysates were made using the enzyme Alcalase^® and the nutritional profile of these hydrolysates was determined. In addition, the bioactive peptide content of developed hydrolysates was identified using mass spectrometry. The potential heart health benefits of developed snail hydrolysates were measured in vitro using the Angiotensin-I-converting Enzyme (ACE-1; EC 3.4.15.1) inhibition assay, and the ACE-1 inhibitory drug Captopril© was used as a positive control. The generated H. aspersa hydrolysates were found to inhibit ACE-1 by 95.60% (±0.011) when assayed at a concentration of 1 mg/mL (n = 9) compared to the positive control Captopril© which inhibited ACE-1 by 96.53% (±0.0156) when assayed at a concentration of 0.005 mg/mL (n = 3). A total of 113 unique peptide sequences were identified following MS analysis with peptides identified ranging from 628.35 Da (peptide GGGLVGGI—protein accession number sp|P54334|XKDO_BACSU) to 2343.14 Da (peptide GPAGVPGLPGAKGDHGFPGSSGRRGD—protein accession number sp|Q7SIB2|CO4A1_BOVIN) in size using the BIOPEP-UWM database. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Figure 1

20 pages, 1090 KiB

Open AccessArticle

Effect of Cooking on Protein Digestion and Antioxidant Activity of Different Legume Pastes

by Marta Gallego, Milagros Arnal, José Manuel Barat and Pau Talens

Foods 2021, 10(1), 47; https://doi.org/10.3390/foods10010047 - 26 Dec 2020

Cited by 27 | Viewed by 4466

Abstract

Legumes are protein-rich foods that can be used to prepare pastes or pureed foods suitable for babies and the elderly. The aims of this study were the characterization of different legume pastes (from soybean, lentil, and pea) subjected to three processing methods (ordinary [...] Read more.

Legumes are protein-rich foods that can be used to prepare pastes or pureed foods suitable for babies and the elderly. The aims of this study were the characterization of different legume pastes (from soybean, lentil, and pea) subjected to three processing methods (ordinary cooking, pressure cooking, and microwave) and the evaluation of protein digestion and antioxidant activity during simulated gastrointestinal digestion (GID). The different cooking methods of legumes led to differences in the physicochemical properties of the pastes, as well as on the textural and viscoelastic characteristics, except for soybean samples, despite all the pastes presenting elastic properties and weak gel behavior. Cooking followed by GID improved the protein digestibility and antioxidant activity of the legumes, which was attributed to released peptides and amino acids more than free phenolics. However, the fate and extent at each digestion stage was different according to the legume type and cooking method, as it would be influenced by the matrix structure and interaction between components. This work has expanded knowledge about the properties, digestibility, and antioxidant activity of different cooked legumes for a future design of pastes. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Graphical abstract

18 pages, 14356 KiB

Open AccessArticle

Spent Hen Protein Hydrolysate with Good Gastrointestinal Stability and Permeability in Caco-2 Cells Shows Antihypertensive Activity in SHR

by Hongbing Fan, Wenlin Yu, Wang Liao and Jianping Wu

Foods 2020, 9(10), 1384; https://doi.org/10.3390/foods9101384 - 01 Oct 2020

Cited by 28 | Viewed by 3660

Abstract

Spent hens are a major byproduct of the egg industry but are rich in muscle proteins that can be enzymatically transformed into bioactive peptides. The present study aimed to develop a spent hen muscle protein hydrolysate (SPH) with antihypertensive activity. Spent hen muscle [...] Read more.

Spent hens are a major byproduct of the egg industry but are rich in muscle proteins that can be enzymatically transformed into bioactive peptides. The present study aimed to develop a spent hen muscle protein hydrolysate (SPH) with antihypertensive activity. Spent hen muscle proteins were hydrolyzed by nine enzymes, either individually or in combination; 18 SPHs were assessed initially for their in vitro angiotensin-converting enzyme (ACE) inhibitory activity, and three SPHs, prepared by Protex 26L (SPH-26L), pepsin (SPH-P), and thermoase (SPH-T), showed promising activity and peptide yield. These three hydrolysates were further assessed for their angiotensin-converting enzyme 2 (ACE2) upregulating, antioxidant, and anti-inflammatory activities; only SPH-T upregulated ACE2 expression, while all three SPHs showed antioxidant and anti-inflammatory activities. During simulated gastrointestinal digestion, ACE2 upregulating, ACE inhibitory and antioxidant activities of SPH-T were not affected, but those of SPH-26L and SPH-P were reduced. ACE inhibitory activity of gastrointestinal-digested SPH-T was not affected after the permeability study in Caco-2 cells, while ACE2 upregulating, antioxidant and anti-inflammatory activities were improved; nine novel peptides with five–eight amino acid residues were identified from the Caco-2 permeate. Among these three hydrolysates, only SPH-T reduced blood pressure significantly when given orally at a daily dose of 1000 mg/kg body weight to spontaneously hypertensive rats. SPH-T can be developed into a promising functional food ingredient against hypertension, contributing to a more sustainable utilization for spent hens while generating extra revenue for the egg industry. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Graphical abstract

14 pages, 1259 KiB

Open AccessArticle

Cocoa (Theobroma cacao L.) Seed Proteins’ Anti-Obesity Potential through Lipase Inhibition Using In Silico, In Vitro and In Vivo Models

by Luis Jorge Coronado-Cáceres, Griselda Rabadán-Chávez, Luis Mojica, Blanca Hernández-Ledesma, Lucía Quevedo-Corona and Eugenia Lugo Cervantes

Foods 2020, 9(10), 1359; https://doi.org/10.3390/foods9101359 - 25 Sep 2020

Cited by 34 | Viewed by 5075

Abstract

The aim of this study was to determine the pancreatic lipase (PL) inhibitory effect of cocoa protein (CP) hydrolysates (CPH) using in silico and in vitro approaches, and an in vivo high-fat diet (HF) obese rat model. The results showed better theoretical affinity [...] Read more.

The aim of this study was to determine the pancreatic lipase (PL) inhibitory effect of cocoa protein (CP) hydrolysates (CPH) using in silico and in vitro approaches, and an in vivo high-fat diet (HF) obese rat model. The results showed better theoretical affinity on PL for cocoa peptides EEQR, GGER, QTGVQ, and VSTDVNIE released from vicilin and albumins (−6.5, −6.3, −6.2, and −6.1 kcal/mol, respectively). Absorption, distribution, metabolism, and excretion (ADMET) prediction showed the human intestinal absorption (HIA) capacity of orlistat and eight cocoa peptides, demonstrating that they presented a low probability of toxicity with values lower than 0.6, while the orlistat has a high probability of hepatotoxicity with a mean value of 0.9. CPH (degree of hydrolysis of 55%) inhibited PL with an IC₅₀ (concentration needed to inhibit 50% of enzyme activity) value of 1.38 mg/mL. The intragastric administration of 150 mg CP/kg/day to rats increased total lipids and triglycerides excretion in feces, ranging from 11% to 15% compared to the HF-diet. The HF + CP-diet also significantly decreased (p < 0.05) the apparent rate of fat absorption compared with the HF group. These results suggest that CP has anti-obesity potential by inhibiting PL, thus helping to prevent the development of non-communicable diseases. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Graphical abstract

22 pages, 1672 KiB

Open AccessArticle

Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products

by Seyadeh Narges Mazloomi, Leticia Mora, M-Concepción Aristoy, Alireza Sadeghi Mahoonak, Mohammad Ghorbani, Gholamreza Houshmand and Fidel Toldrá

Foods 2020, 9(9), 1217; https://doi.org/10.3390/foods9091217 - 02 Sep 2020

Cited by 16 | Viewed by 3018

Abstract

In this study, orange seed proteins were hydrolyzed by Alcalase enzyme at different enzyme concentrations 1–3% (v/w) and hydrolysis times (2–5 h), to obtain bioactive peptides showing antioxidant, Angiotensin-converting enzyme (ACE) -inhibitory, and hypoglycemic activities. The highest biological activities [...] Read more.

In this study, orange seed proteins were hydrolyzed by Alcalase enzyme at different enzyme concentrations 1–3% (v/w) and hydrolysis times (2–5 h), to obtain bioactive peptides showing antioxidant, Angiotensin-converting enzyme (ACE) -inhibitory, and hypoglycemic activities. The highest biological activities (p < 0.05) were achieved by using a hydrolysis time of 5 h and an enzyme concentration of 2%. Orange seed protein hydrolysate (OSPH) was prepared under these conditions, and peptides were isolated and purified by using size-exclusion chromatography and high-performance liquid chromatography, respectively. The fractions that showed the highest biological activities were analyzed by mass spectrometry in tandem, and a total of 63 peptide sequences were found. Moreover, the effect of simulated gastrointestinal digestion on the bioactivity of the fractions was studied, and the novel peptide sequences generated were also identified. Overall, despite there being some differences in the profile of peptide sequences obtained, the main results showed non-significant differences in the analyzed bioactivities after simulated gastrointestinal digestion. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Graphical abstract

12 pages, 746 KiB

Open AccessArticle

Identification and Antimicrobial Activity of Medium-Sized and Short Peptides from Yellowfin Tuna (Thunnus albacares) Simulated Gastrointestinal Digestion

by Andrea Cerrato, Anna Laura Capriotti, Federico Capuano, Chiara Cavaliere, Angela Michela Immacolata Montone, Carmela Maria Montone, Susy Piovesana, Riccardo Zenezini Chiozzi and Aldo Laganà

Foods 2020, 9(9), 1185; https://doi.org/10.3390/foods9091185 - 27 Aug 2020

Cited by 23 | Viewed by 3963

Abstract

Due to the rapidly increasing resistance to conventional antibiotics, antimicrobial peptides are emerging as promising novel drug candidates. In this study, peptide fragments were obtained from yellowfin tuna muscle by simulated gastrointestinal digestion, and their antimicrobial activity towards Gram-positive and Gram-negative bacteria was [...] Read more.

Due to the rapidly increasing resistance to conventional antibiotics, antimicrobial peptides are emerging as promising novel drug candidates. In this study, peptide fragments were obtained from yellowfin tuna muscle by simulated gastrointestinal digestion, and their antimicrobial activity towards Gram-positive and Gram-negative bacteria was investigated. In particular, the antimicrobial activity of both medium- and short-sized peptides was investigated by using two dedicated approaches. Medium-sized peptides were purified by solid phase extraction on C18, while short peptides were purified thanks to a graphitized carbon black sorbent. For medium-sized peptide characterization, a peptidomic strategy based on shotgun proteomics analysis was employed, and identification was achieved by matching protein sequence database by homology, as yellowfin tuna is a non-model organism, leading to the identification of 403 peptides. As for short peptide sequences, an untargeted suspect screening approach was carried out by means of an inclusion list presenting the exact mass to charge ratios (m/z) values for all di-, tri- and tetrapeptides. In total, 572 short sequences were identified thanks to a customized workflow dedicated to short peptide analysis implemented on Compound Discoverer software. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Graphical abstract

13 pages, 2842 KiB

Open AccessArticle

Analysis of Narrow-Leaf Lupin Proteins in Lupin-Enriched Pasta by Untargeted and Targeted Mass Spectrometry

by Gilda Aiello, Yuchen Li, Giovanna Boschin, Marco Stanziale, Carmen Lammi and Anna Arnoldi

Foods 2020, 9(8), 1083; https://doi.org/10.3390/foods9081083 - 08 Aug 2020

Cited by 6 | Viewed by 2652

Abstract

The supplementation of different food items with grain legumes and, in particular, with lupin has been demonstrated to provide useful health benefits, especially in the area of cardiovascular disease prevention. In this work, label free quantitative untargeted and targeted approaches based on liquid [...] Read more.

The supplementation of different food items with grain legumes and, in particular, with lupin has been demonstrated to provide useful health benefits, especially in the area of cardiovascular disease prevention. In this work, label free quantitative untargeted and targeted approaches based on liquid chromatography−electrospray ionization−tandem mass spectrometry (LC−ESI−MS/MS) for investigating the protein profile of three pasta samples containing different percentages of narrow-leaf lupin flour were carried out. The untargeted method permitted the identification of the main acidic globulins (α-conglutin, β-conglutin, and δ-conglutin) and the comparison of their profile with raw lupin flour. The targeted method, based on High-performance liquid chromatography electrospray ionization tandem mass spectrometry HPLC-Chip-Multiple Reaction Monitoring (MRM) mode, allowed the quantification of γ-conglutin, the main hypoglycemic component of lupin protein: its concentration was around 2.25 mg/g in sample A, 2.16 mg/g in sample D, and 0.57 mg/g in sample F. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Figure 1

33 pages, 1052 KiB

Open AccessArticle

Characteristics of Biopeptides Released In Silico from Collagens Using Quantitative Parameters

by Anna Iwaniak, Piotr Minkiewicz, Monika Pliszka, Damir Mogut and Małgorzata Darewicz

Foods 2020, 9(7), 965; https://doi.org/10.3390/foods9070965 - 21 Jul 2020

Cited by 27 | Viewed by 3988

Abstract

The potential of collagens to release biopeptides was evaluated using the BIOPEP-UWM-implemented quantitative criteria including the frequency of the release of fragments with a given activity by selected enzyme(s) (A_E), relative frequency of release of fragments with a given activity by [...] Read more.

The potential of collagens to release biopeptides was evaluated using the BIOPEP-UWM-implemented quantitative criteria including the frequency of the release of fragments with a given activity by selected enzyme(s) (A_E), relative frequency of release of fragments with a given activity by selected enzyme(s) (W), and the theoretical degree of hydrolysis (DH_t). Cow, pig, sheep, chicken, duck, horse, salmon, rainbow trout, goat, rabbit, and turkey collagens were theoretically hydrolyzed using: stem bromelain, ficin, papain, pepsin, trypsin, chymotrypsin, pepsin+trypsin, and pepsin+trypsin+chymotrypsin. Peptides released from the collagens having comparable A_E and W were estimated for their likelihood to be bioactive using PeptideRanker Score. The collagens tested were the best sources of angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitors. A_E and W values revealed that pepsin and/or trypsin were effective producers of such peptides from the majority of the collagens examined. Then, the SwissTargetPrediction program was used to estimate the possible interactions of such peptides with enzymes and proteins, whereas ADMETlab was applied to evaluate their safety and drug-likeness properties. Target prediction revealed that the collagen-derived peptides might interact with several human proteins, especially proteinases, but with relatively low probability. In turn, their bioactivity may be limited by their short half-life in the body. Full article

(This article belongs to the Special Issue Proteins and Bioactive Peptides in High Protein Content Foods)

► Show Figures

Graphical abstract

Journal Menu

Journal Browser

Proteins and Bioactive Peptides in High Protein Content Foods

Share This Special Issue

Special Issue Editors

Special Issue Information

Keywords

Published Papers (9 papers)

Editorial

Research

Further Information

Guidelines

MDPI Initiatives

Follow MDPI