Role of Enzymatic Modification on the Antioxidant Activity of Proteins

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 10057

Special Issue Editors


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Guest Editor
Department of Biological Sciences, School of Natural Sciences, Faculty of Science and Engineering, University of Limerick, Limerick V94 T9PX, Ireland
Interests: protein biochemistry; bioactive peptides; biofunctional proteins; plant proteins; protein ingredients; phenolic compounds; sustainable food ingredients; food formulation; food processing

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Guest Editor
Department of Biological Sciences School of Natural Sciences, Faculty of Science and Engineering, University of Limerick, Limerick V94 T9PX, Ireland
Interests: functional food ingredients; application of proteolytic enzymes; technofunctional ingredient; bioactive ingredients; biorefinery of food and agricultural wastes; food processing; food product development

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Guest Editor
Department of Biological Sciences, School of Natural Sciences, Faculty of Science and Engineering, University of Limerick, Limerick V94 T9PX, Ireland
Interests: food protein ingredients; functional food ingredients/nutraceuticals; food protein chemistry/biochemistry; enzymatic hydrolysis of food proteins; bioactive peptides; enzymatic cross-linking of food proteins; purification and characterization of starter culture-derived aminopeptidases; role of aminopeptidases in food protein hydrolysate debittering

Special Issue Information

Dear Colleagues,

Proteins are considered one of the most important macromolecules in living systems. Within their multiple functions, proteins and their associated enzymatically modified derivatives have been reported to act as antioxidant agents. Enzymatic modification of proteins, e.g., hydrolysis, conjugation, deamidation, cross-linking, etc., can enhance their antioxidant activity.

This property may have many benefits, including applications as control/management agents for oxidative stress as part of our dietary intake, as antiaging agents in the cosmetic industry, and as general preservatives in the food industry.

Antioxidant agents can neutralize free radicals and reactive oxygen species (ROS). Some protein derivatives, particularly hydrolysates and peptides, have been reported to induce the release of antioxidant compounds/enzymes such as glutathione (GSH), superoxide dismutase (SOD) and catalase (CAT). These have been associated with the regulation of oxidative stress at a cellular level. Furthermore, the antioxidant activity associated with proteins/peptides may contribute to minimization of lipid oxidation in foods. Therefore, there is considerable current interest in the study and application of proteins and their enzymatically modified derivatives in the prevention and management of oxidation reactions. 

Submissions to this Special Issue on the “Role of Enzymatic Modification on the Antioxidant Activity of Proteins” are welcome in the form of original research papers or review articles that cover the following topics:

  • In vitro, in situ/ex vivo, and/or in vivo assessment of the antioxidant potency of proteins and their enzymatically modified derivatives, e.g., peptides;
  • Evidence of the role of enzymatic modification of proteins from different sources, e.g., dairy, plant, animal, insect, on their antioxidant activity in vitro, in situ/ex vivo and/or in vivo;
  • Novel enzymatic approaches to enhance the antioxidant activity of proteins;
  • Impact of processing (e.g., physical/thermal treatments) on the antioxidant activity of enzymatically modified protein ingredients;
  • Application of enzymatically modified protein ingredients as antioxidant agents in the preservation of food and non-food products.

Dr. Maria Cermeño
Dr. Thanyaporn Kleekayai
Prof. Dr. Richard J. FitzGerald
Guest Editors

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Keywords

  • antioxidant
  • enzymatic modification
  • protein
  • oxidative stress
  • peptide
  • antiaging
  • oxidation

Published Papers (3 papers)

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Research

17 pages, 3165 KiB  
Article
Ultrafiltration of Saithe (Pollachius virens) Protein Hydrolysates and Its Effect on Antioxidative Activity
by Veronica Hjellnes, Turid Rustad, Ida-Johanne Jensen, Elin Eiken, Stine Marie Pettersen and Eva Falch
Catalysts 2021, 11(9), 1053; https://doi.org/10.3390/catal11091053 - 30 Aug 2021
Cited by 9 | Viewed by 2365
Abstract
The whitefish industry generates a huge amount of rest raw material, which is currently wasted or underutilized in the production of low-value products such as animal feed. While fish muscle is the primary product of use for human consumption, rest raw material has [...] Read more.
The whitefish industry generates a huge amount of rest raw material, which is currently wasted or underutilized in the production of low-value products such as animal feed. While fish muscle is the primary product of use for human consumption, rest raw material has great potential as a source of protein and bioactive peptides for the production of food ingredients and nutraceuticals. Enzymatic hydrolysis is a biotechnological processing method that can be used to extract protein from fish rest raw material into a protein hydrolysate. This study aimed at investigating the functionality of ultrafiltration as an industrial processing method and its effect on the bioactivity of protein hydrolysates. Protein hydrolysates were produced by enzymatic hydrolysis of saithe (Pollachius virens) head and backbone caught at two separate occasions to investigate the effect of seasonal variations. Ultrafiltration effectively concentrated larger peptides (>4 kDa) and smaller peptides (<4 kDa) in separate fractions, with a protein yield of 31% in the fraction <4 kDa. The unfiltered hydrolysate was found to have a higher antioxidative activity compared to the <4 kDa fraction in ABTS, FRAP, and ORAC assays. These results indicate that ultrafiltration does not effectively increase bioactivity by concentrating small peptides and that bioactivity is dependent on several properties, including interaction with larger peptides. Full article
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12 pages, 1452 KiB  
Article
Preliminary Study of Extended Ripening Effects on Peptides Evolution and DPPH Radical Scavenging Activity in Mexican Goat Cheese
by Rosa Vázquez-García, Anaberta Cardador-Martínez, Miguel Angel Orihuela-López, Livia Sofía Ramos-Hernández and Sandra Teresita Martín-del-Campo
Catalysts 2021, 11(8), 967; https://doi.org/10.3390/catal11080967 - 12 Aug 2021
Cited by 3 | Viewed by 1751
Abstract
Cheese ripening causes intense proteolysis, particularly when the cheese contains starter cultures. Several studies have shown the presence of bioactive peptides in goat’s milk cheeses with antioxidant activity. Mexican goat cheeses’ peptide fractions were evaluated at different ripening stages. Additionally, they were correlated [...] Read more.
Cheese ripening causes intense proteolysis, particularly when the cheese contains starter cultures. Several studies have shown the presence of bioactive peptides in goat’s milk cheeses with antioxidant activity. Mexican goat cheeses’ peptide fractions were evaluated at different ripening stages. Additionally, they were correlated with their antioxidant activity. Proteolysis was measured in the acid-soluble nitrogen and non-protein nitrogen fractions using reverse-phase high-performance liquid chromatography. While the antioxidant activity in both nitrogenous fractions was determined using a 2,2-diphenyl-1-picrylhydrazyl solution. Analyzed cheeses showed peptides fraction in the retention time of 2.05, 18.36, and 50.11 min for acid-soluble fraction and non-protein protein nitrogen, and showed antioxidant activity from the first day of ripening to 73% discoloration in the DPPH solution at 55 ripening days. Obtained results suggested that ripened Mexican goat cheese had a DPPH radical scavenging activity related to peptides present originally in the milk or released by starter culture action during cheese ripening. Full article
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15 pages, 1506 KiB  
Article
In Vitro Digestibility and Antioxidant Activity of Plant Protein Isolate and Milk Protein Concentrate Blends
by Mohammadreza Khalesi and Richard J. FitzGerald
Catalysts 2021, 11(7), 787; https://doi.org/10.3390/catal11070787 - 28 Jun 2021
Cited by 22 | Viewed by 4943
Abstract
The replacement of animal with plant proteins in human diets has been increasing in recent years. The impact of blending milk protein concentrate (MPC) with protein isolates from soy (SPI), rice (RPI) and pea (PPI) on the in vitro digestibility and antioxidant activity [...] Read more.
The replacement of animal with plant proteins in human diets has been increasing in recent years. The impact of blending milk protein concentrate (MPC) with protein isolates from soy (SPI), rice (RPI) and pea (PPI) on the in vitro digestibility and antioxidant activity of the resultant blends was investigated. Different plant protein–MPC blends (i.e., SPI–MPC (25:75), RPI–MPC (50:50) and PPI–MPC (25:75)) were analyzed. The lowest protein digestibility corrected amino acid score (PDCAAS) was associated with RPI (0.70), while the blends had PDCAAS values above 1.00 demonstrating the high digestibility of the proteins in the blends studied. An in vitro simulated gastrointestinal digestion was carried out on the samples. The degree of hydrolysis and gel permeation high performance liquid chromatography profiles showed that the SPI–MPC blend was more extensively digested in the gastric phase compared with the two other blends, while the PPI–MPC and RPI–MPC blends were mainly digested during the intestinal phase. The SPI–MPC digested blend had the highest 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity having a half maximal effective concentration (EC50) of 0.10 ± 0.01 mg/mL. The findings show that blends of plant protein with MPC had higher in vitro digestibility and antioxidant activity compared to the individual plant protein isolates. Full article
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