Editorial

3 pages, 174 KiB

Open AccessEditorial

Introduction to the Special Issue: New Advances in the Research of Antioxidant Food Peptides

by Lourdes Amigo and Blanca Hernández-Ledesma

Foods 2020, 9(12), 1810; https://doi.org/10.3390/foods9121810 - 07 Dec 2020

Viewed by 1181

During cell metabolism, oxygen is partially reduced to reactive oxygen species (ROS) that play a physiological role in cellular processes, including proliferation, cell cycle and death, and signal transduction [...] Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

Research

Jump to: Editorial, Review

15 pages, 2356 KiB

Open AccessArticle

Antioxidant Potential of Mung Bean (Vigna radiata) Albumin Peptides Produced by Enzymatic Hydrolysis Analyzed by Biochemical and In Silico Methods

by Jennifer Kusumah, Luis M. Real Hernandez and Elvira Gonzalez de Mejia

Foods 2020, 9(9), 1241; https://doi.org/10.3390/foods9091241 - 04 Sep 2020

Cited by 23 | Viewed by 5674

Abstract

The objective of this study was to investigate the biochemical antioxidant potential of peptides derived from enzymatically hydrolyzed mung bean (Vigna radiata) albumins using an 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assay, a ferrous ion chelating assay and an oxygen radical absorbance capacity [...] Read more.

The objective of this study was to investigate the biochemical antioxidant potential of peptides derived from enzymatically hydrolyzed mung bean (Vigna radiata) albumins using an 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assay, a ferrous ion chelating assay and an oxygen radical absorbance capacity (ORAC) assay. Peeled raw mung bean was ground into flour and mixed with buffer (pH 8.3, 1:20 w/v ratio) before being stirred, then filtered using 3 kDa and 30 kDa molecular weight cut-off (MWCO) centrifugal filters to obtain albumin fraction. The albumin fraction then underwent enzymatic hydrolysis using either gastrointestinal enzymes (pepsin and pancreatin) or thermolysin. Peptides in the hydrolysates were sequenced. The peptides showed low ABTS radical-scavenging activity (90–100 μg ascorbic acid equivalent/mL) but high ferrous ion chelating activity (1400–1500 μg EDTA equivalent/mL) and ORAC values (>120 μM Trolox equivalent). The ferrous ion chelating activity was enzyme- and hydrolysis time-dependent. For thermolysin hydrolysis, there was a drastic increase in ferrous ion chelating activity from t = 0 (886.9 μg EDTA equivalent/mL) to t = 5 min (1559.1 μg EDTA equivalent/mL) before plateauing. For pepsin–pancreatin hydrolysis, there was a drastic decrease from t = 0 (878.3 μg EDTA equivalent/mL) to t = 15 (138.0 μg EDTA equivalent/mL) after pepsin was added, but this increased from t = 0 (131.1 μg EDTA equivalent/mL) to t = 15 (1439.2 μg EDTA equivalent/mL) after pancreatin was added. There was no significant change in ABTS radical scavenging activity or ORAC values throughout different hydrolysis times for either the thermolysin or pepsin–pancreatin hydrolysis. Overall, mung bean hydrolysates produced peptides with high potential antioxidant capacity, being particularly effective ferrous ion chelators. Other antioxidant assays that use cellular lines should be performed to measure antioxidant capacity before animal and human studies. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

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17 pages, 1387 KiB

Open AccessFeature PaperArticle

In Silico and In Vitro Analysis of Multifunctionality of Animal Food-Derived Peptides

by Lourdes Amigo, Daniel Martínez-Maqueda and Blanca Hernández-Ledesma

Foods 2020, 9(8), 991; https://doi.org/10.3390/foods9080991 - 24 Jul 2020

Cited by 30 | Viewed by 4093

Abstract

Currently, the associations between oxidative stress, inflammation, hypertension, and metabolic disturbances and non-communicable diseases are very well known. Since these risk factors show a preventable character, the searching of food peptides acting against them has become a promising strategy for the design and [...] Read more.

Currently, the associations between oxidative stress, inflammation, hypertension, and metabolic disturbances and non-communicable diseases are very well known. Since these risk factors show a preventable character, the searching of food peptides acting against them has become a promising strategy for the design and development of new multifunctional foods or nutraceuticals. In the present study, an integrated approach combining an in silico study and in vitro assays was used to confirm the multifunctionality of milk and meat protein-derived peptides that were similar to or shared amino acids with previously described opioid peptides. By the in silico analysis, 15 of the 27 assayed peptides were found to exert two or more activities, with Angiotensin-converting enzyme (ACE) inhibitory, antioxidant, and opioid being the most commonly found. The in vitro study confirmed ACE-inhibitory and antioxidant activities in 15 and 26 of the 27 synthetic peptides, respectively. Four fragments, RYLGYLE, YLGYLE, YFYPEL, and YPWT, also demonstrated the ability to protect Caco-2 and macrophages RAW264.7 cells from the oxidative damage caused by chemicals. The multifunctionality of these peptides makes them promising agents against oxidative stress-associated diseases. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

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22 pages, 4032 KiB

Open AccessArticle

In Vitro Characterisation of the Antioxidative Properties of Whey Protein Hydrolysates Generated under pH- and Non pH-Controlled Conditions

by Thanyaporn Kleekayai, Aurélien V. Le Gouic, Barbara Deracinois, Benoit Cudennec and Richard J. FitzGerald

Foods 2020, 9(5), 582; https://doi.org/10.3390/foods9050582 - 05 May 2020

Cited by 24 | Viewed by 3037

Abstract

Bovine whey protein concentrate (WPC) was hydrolysed under pH-stat (ST) and non pH-controlled (free-fall, FF) conditions using Debitrase (DBT) and FlavorPro Whey (FPW). The resultant whey protein hydrolysates (WPHs) were assessed for the impact of hydrolysis conditions on the physicochemical and the in [...] Read more.

Bovine whey protein concentrate (WPC) was hydrolysed under pH-stat (ST) and non pH-controlled (free-fall, FF) conditions using Debitrase (DBT) and FlavorPro Whey (FPW). The resultant whey protein hydrolysates (WPHs) were assessed for the impact of hydrolysis conditions on the physicochemical and the in vitro antioxidant and intracellular reactive oxygen species (ROS) generation in oxidatively stressed HepG2 cells. Enzyme and hydrolysis condition dependent differences in the physicochemical properties of the hydrolysates were observed, however, the extent of hydrolysis was similar under ST and FF conditions. Significantly higher (p < 0.05) in vitro and cellular antioxidant activities were observed for the DBT compared to the FPW–WPHs. The WPHs generated under ST conditions displayed significantly higher (p < 0.05) oxygen radical absorbance capacity (ORAC) and Trolox equivalent antioxidant capacity (TEAC) values compared to the FF-WPHs. The impact of hydrolysis conditions was more pronounced in the in vitro compared to the cellular antioxidant assay. WPH peptide profiles (LC-MS/MS) were also enzyme and hydrolysis conditions dependent as illustrated in the case of β-lactoglobulin. Therefore, variation in the profiles of the peptides released may explain the observed differences in the antioxidant activity. Targeted generation of antioxidant hydrolysates needs to consider the hydrolysis conditions and the antioxidant assessment method employed. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

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12 pages, 1281 KiB

Open AccessArticle

Antioxidant and Anti-Apoptotic Properties of Oat Bran Protein Hydrolysates in Stressed Hepatic Cells

by Ramak Esfandi, William G. Willmore and Apollinaire Tsopmo

Foods 2019, 8(5), 160; https://doi.org/10.3390/foods8050160 - 11 May 2019

Cited by 16 | Viewed by 4461

Abstract

The objective of this work was to find out how the method to extract proteins and subsequent enzymatic hydrolysis affect the ability of hepatic cells to resist oxidative stress. Proteins were isolated from oat brans in the presence of Cellulase (CPI) or Viscozyme [...] Read more.

The objective of this work was to find out how the method to extract proteins and subsequent enzymatic hydrolysis affect the ability of hepatic cells to resist oxidative stress. Proteins were isolated from oat brans in the presence of Cellulase (CPI) or Viscozyme (VPI). Four protein hydrolysates were produced from CPI and four others from VPI when they treated with Alcalase, Flavourzyme, Papain, or Protamex. Apart from CPI-Papain that reduced the viability of cell by 20%, no other hydrolysate was cytotoxic in the hepatic HepG2 cells. In the cytoprotection test, VPI-Papain and VPI-Flavourzyme fully prevented the damage due to peroxyl radical while CPI-Papain and CPI-Alcalase enhanced the cellular damage. Cells treated with VPI-hydrolysates reduced intracellular reactive oxygen species (ROS) by 20–40% and, also increased the intracellular concentration of glutathione, compared to CPI-hydrolysates. In antioxidant enzyme assays, although all hydrolysates enhanced the activity of both superoxide dismutase and catalase by up to 2- and 3.4-fold, respectively relative the control cells, the largest increase was due to VPI-Papain and VPI-Flavourzyme hydrolysates. In caspase-3 assays, hydrolysates with reduced ROS or enhanced antioxidant enzyme activities were able to reduce the activity of the pro-apoptotic enzyme, caspase-3 indicating that they prevented oxidative stress-induced cell death. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

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Review

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30 pages, 887 KiB

Open AccessReview

Extraction and Characterization of Antioxidant Peptides from Fruit Residues

by Saúl Olivares-Galván, María Luisa Marina and María Concepción García

Foods 2020, 9(8), 1018; https://doi.org/10.3390/foods9081018 - 29 Jul 2020

Cited by 18 | Viewed by 5981

Abstract

Fruit residues with high protein contents are generated during the processing of some fruits. These sustainable sources of proteins are usually discarded and, in all cases, underused. In addition to proteins, these residues can also be sources of peptides with protective effects against [...] Read more.

Fruit residues with high protein contents are generated during the processing of some fruits. These sustainable sources of proteins are usually discarded and, in all cases, underused. In addition to proteins, these residues can also be sources of peptides with protective effects against oxidative damage. The revalorization of these residues, as sources of antioxidant peptides, requires the development of suitable methodologies for their extraction and the application of analytical techniques for their characterization. The exploitation of these residues involves two main steps: the extraction and purification of proteins and their hydrolysis to release peptides. The extraction of proteins is mainly carried out under alkaline conditions and, in some cases, denaturing reagents are also employed to improve protein solubilization. Alternatively, more sustainable strategies based on the use of high-intensity focused ultrasounds, microwaves, pressurized liquids, electric fields, or discharges, as well as deep eutectic solvents, are being implemented for the extraction of proteins. The scarce selectivity of these extraction methods usually makes the subsequent purification of proteins necessary. The purification of proteins based on their precipitation or the use of ultrafiltration has been the usual procedure, but new strategies based on nanomaterials are also being explored. The release of potential antioxidant peptides from proteins is the next step. Microbial fermentation and, especially, digestion with enzymes such as Alcalase, thermolysin, or flavourzyme have been the most common. Released peptides are next characterized by the evaluation of their antioxidant properties and the application of proteomic tools to identify their sequences. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

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25 pages, 369 KiB

Open AccessReview

Whey for Sarcopenia; Can Whey Peptides, Hydrolysates or Proteins Play a Beneficial Role?

by Sarah Gilmartin, Nora O’Brien and Linda Giblin

Foods 2020, 9(6), 750; https://doi.org/10.3390/foods9060750 - 05 Jun 2020

Cited by 28 | Viewed by 6162

Abstract

As the human body ages, skeletal muscle loses its mass and strength. It is estimated that in 10% of individuals over the age of 60, this muscle frailty has progressed to sarcopenia. Biomarkers of sarcopenia include increases in inflammatory markers and oxidative stress [...] Read more.

As the human body ages, skeletal muscle loses its mass and strength. It is estimated that in 10% of individuals over the age of 60, this muscle frailty has progressed to sarcopenia. Biomarkers of sarcopenia include increases in inflammatory markers and oxidative stress markers and decreases in muscle anabolic markers. Whey is a high-quality, easily digested dairy protein which is widely used in the sports industry. This review explores the evidence that whey protein, hydrolysates or peptides may have beneficial effects on sarcopenic biomarkers in myoblast cell lines, in aged rodents and in human dietary intervention trials with the older consumer. A daily dietary supplementation of 35 g of whey is likely to improve sarcopenic biomarkers in frail or sarcopenia individuals. Whey supplementation, consumed by an older, healthy adult certainly improves muscle mTOR signaling, but exercise appears to have the greatest benefit to older muscle. In vitro cellular assays are central for bioactive and bioavailable peptide identification and to determine their mechanism of action on ageing muscle. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

16 pages, 333 KiB

Open AccessReview

Chicken Egg Proteins and Derived Peptides with Antioxidant Properties

by Sara Benedé and Elena Molina

Foods 2020, 9(6), 735; https://doi.org/10.3390/foods9060735 - 03 Jun 2020

Cited by 54 | Viewed by 7524

Abstract

In addition to their high nutritional value, some chicken egg proteins and derivatives such as protein hydrolysates, peptides and amino acids show antioxidant properties which make them prominent candidates for the development of functional foods, drawing attention to both the food and biopharmaceutical [...] Read more.

In addition to their high nutritional value, some chicken egg proteins and derivatives such as protein hydrolysates, peptides and amino acids show antioxidant properties which make them prominent candidates for the development of functional foods, drawing attention to both the food and biopharmaceutical industries. This review summarizes current knowledge on antioxidant activity of chicken egg proteins and their derived peptides. Some egg proteins such as ovalbumin, ovotransferrin and lysozyme from egg white or phosvitin from yolk have shown antioxidant properties, although derived peptides have higher bioactive potential. The main process for obtaining egg bioactive peptides is enzymatic hydrolysis of its proteins using enzymes and/or processing technologies such as heating, sonication or high-intensity-pulsed electric field. Different in vitro assays such as determination of reducing power, DPPH and ABTS radical-scavenging activity tests or oxygen radical absorbance capacity assay have been used to evaluate the diverse antioxidant mechanisms of proteins and peptides. Similarly, different cell lines and animal models including zebrafish, mice and rats have also been used. In summary, this review collects all the knowledge described so far regarding egg proteins and derived peptides with antioxidant functions. Full article

(This article belongs to the Special Issue New Advances in the Research of Antioxidant Food Peptides)

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