Structural Characterization of Food Proteins and Peptides

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Physics and (Bio)Chemistry".

Deadline for manuscript submissions: 31 August 2024 | Viewed by 6748

Special Issue Editors


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Guest Editor
Department of Chemical Sciences, Laboratory of Organic Mass Spectrometry (LOMS), University of Catania, 95126 Catania, Italy
Interests: food proteins; bioactive peptides; milk proteins; LC/MS-MS; high-resolution mass spectrometry; proteomics; paleoproteomics

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Guest Editor
Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125 Catania, Italy
Interests: mass spectrometry; NMR; chromatographic separation; natural products chemistry; proteomics; food analysis; organic chemistry
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
Department of Chemical Sciences, Laboratory of Organic Mass Spectrometry (LOMS), University of Catania, Catania, Italy
Interests: ultra HPLC; high-resolution mass spectrometry; proteomics; food proteins; wheat proteins; post-translational modifications of voltage-dependent anion selective channel isoforms (VDACs)

Special Issue Information

Dear Colleagues,

In recent decades, the agrifood sector, due to the globalization and the development of new technologies, is undergoing important changes that require a deeper characterization of the food chain, starting from raw materials up to the final products. In addition, consumers are concerned about the food that they eat and ask for more assurances on quality, safety, and geographical origin of the products that they consume. There is no doubt that proteins represent the key factor in the human diet, primarily sourced from animals and plants such as dairy, cereals, fish, and meat. Characterization of the protein fraction in foodstuffs may help us to understand the relationship between the protein content and the nutritional and technological properties of foods, for designing new strategies for food traceability, quality, and safety, and also for identifying genetically modified products and microbial contaminants. Moreover, considering the widespread presence of allergenic proteins in some of the most extensively eaten food (i.e., milk, eggs, cereals, etc.), it is clear how the detection of allergenic proteins represents a powerful tool for food control, providing the basis for the production of hypo-allergenic or nutraceutical foods (Pharma-Foods).

Prof. Dr. Vincenzo Cunsolo
Dr. Vera Muccilli
Prof. Dr. Rosaria Saletti
Guest Editors

Manuscript Submission Information

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Keywords

  • Foods
  • Proteins
  • Peptides
  • Bioactive compounds
  • Proteomics
  • Food allergy
  • Food traceability
  • Food safety

Published Papers (4 papers)

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Research

18 pages, 1805 KiB  
Article
Mass Spectrometry Characterization of the SDS-PAGE Protein Profile of Legumins and Vicilins from Chickpea Seed
by Antonella Di Francesco, Michele Andrea De Santis, Aldo Lanzoni, Maria Gaetana Giovanna Pittalà, Rosaria Saletti, Zina Flagella and Vincenzo Cunsolo
Foods 2024, 13(6), 887; https://doi.org/10.3390/foods13060887 - 14 Mar 2024
Viewed by 678
Abstract
Chickpea (Cicer arietinum L.) seed proteins show a lot of functional properties leading this legume to be an interesting component for the development of protein-enriched foods. However, both the in-depth proteomic investigation and structural characterization of chickpea seed proteins are still lacking. [...] Read more.
Chickpea (Cicer arietinum L.) seed proteins show a lot of functional properties leading this legume to be an interesting component for the development of protein-enriched foods. However, both the in-depth proteomic investigation and structural characterization of chickpea seed proteins are still lacking. In this paper a detailed characterization of chickpea seed protein fraction by means of SDS-PAGE, in-gel protein digestion, high-resolution mass spectrometry, and database searching is reported. Through this approach, twenty SDS gel bands were cut and analyzed. While the majority of the bands and the identified peptides were related to vicilin and legumin storage proteins, metabolic functional proteins were also detected. Legumins, as expected, were revealed at 45–65 kDa, as whole subunits with the α- and β-chains linked together by a disulphide bond, but also at lower mass ranges (α- and β-chains migrating alone). Similarly, but not expected, the vicilins were also spread along the mass region between 65 and 23 kDa, with some of them being identified in several bands. An MS structural characterization allowed to determine that, although chickpea vicilins were always described as proteins lacking cysteine residues, they contain this amino acid residue. Moreover, similar to legumins, these storage proteins are firstly synthesized as pre-propolypeptides (Mr 50–80 kDa) that may undergo proteolytic steps that not only cut the signal peptides but also produce different subunits with lower molecular masses. Overall, about 360 different proteins specific of the Cicer arietinum L. species were identified and characterized, a result that, up to the current date, represents the most detailed description of the seed proteome of this legume. Full article
(This article belongs to the Special Issue Structural Characterization of Food Proteins and Peptides)
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17 pages, 2605 KiB  
Article
Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
by Teodora Đukić, Katarina Smiljanić, Jelena Mihailović, Ivana Prodić, Danijela Apostolović, Shu-Hua Liu, Michelle M. Epstein, Marianne van Hage, Dragana Stanić-Vučinić and Tanja Ćirković Veličković
Foods 2022, 11(24), 3993; https://doi.org/10.3390/foods11243993 - 09 Dec 2022
Cited by 4 | Viewed by 1838
Abstract
Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. [...] Read more.
Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs. Full article
(This article belongs to the Special Issue Structural Characterization of Food Proteins and Peptides)
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16 pages, 4016 KiB  
Article
Structural Analysis and Study of Gel Properties of Thermally-Induced Soybean Isolate–Potato Protein Gel System
by Fengqiujie Wang, Xuelian Gu, Mingshou Lü, Yuyang Huang, Ying Zhu, Ying Sun and Xiuqing Zhu
Foods 2022, 11(22), 3562; https://doi.org/10.3390/foods11223562 - 09 Nov 2022
Cited by 3 | Viewed by 1930
Abstract
Heat-induced composite gel systems consisting of different soybean protein isolate (SPI) and potato protein (PP) mixtures were studied to elucidate their “backbone” and property changes. This was achieved by comparing the ratio of non-network proteins, protein subunit composition, and aggregation of different gel [...] Read more.
Heat-induced composite gel systems consisting of different soybean protein isolate (SPI) and potato protein (PP) mixtures were studied to elucidate their “backbone” and property changes. This was achieved by comparing the ratio of non-network proteins, protein subunit composition, and aggregation of different gel samples. It was revealed that SPI was the “gel network backbone” and PP played the role of “filler” in the SPI-PP composite gel system. Compared with the composite gels at the same ratio, springiness and WHC decrease with PP addition. For hardness, PP addition showed a less linear trend. At the SPI-PP = 2/1 composite gel, hardness was more than doubled, while springiness and WHC did not decrease too much and increased the inter-protein binding. The hydrophobic interactions and electrostatic interactions and hydrogen bonding of the SPI gel system were enhanced. The scanning electron microscopy results showed that the SPI-based gel system was able to form a more compact and compatible gel network. This study demonstrates the use of PP as a potential filler that can effectively improve the gelling properties of SPI, thus providing a theoretical basis for the study of functional plant protein foods. Full article
(This article belongs to the Special Issue Structural Characterization of Food Proteins and Peptides)
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9 pages, 1193 KiB  
Article
Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1
by Linda Ahammer, Jana Unterhauser, Reiner Eidelpes, Christina Meisenbichler, Bettina Nothegger, Claudia E. Covaciu, Valentina Cova, Anna S. Kamenik, Klaus R. Liedl, Kathrin Breuker, Klaus Eisendle, Norbert Reider, Thomas Letschka and Martin Tollinger
Foods 2022, 11(19), 2953; https://doi.org/10.3390/foods11192953 - 21 Sep 2022
Cited by 1 | Viewed by 1192
Abstract
The protein Mal d 1 is responsible for most allergic reactions to apples (Malus domestica) in the northern hemisphere. Mal d 1 contains a cysteine residue on its surface, with its reactive side chain thiol exposed to the surrounding food matrix. [...] Read more.
The protein Mal d 1 is responsible for most allergic reactions to apples (Malus domestica) in the northern hemisphere. Mal d 1 contains a cysteine residue on its surface, with its reactive side chain thiol exposed to the surrounding food matrix. We show that, in vitro, this cysteine residue is prone to spontaneous chemical modification by ascorbic acid (vitamin C). Using NMR spectroscopy and mass spectrometry, we characterize the chemical structure of the cysteine adduct and provide a three-dimensional structural model of the modified apple allergen. The S-ascorbylated cysteine partially masks a major IgE antibody binding site on the surface of Mal d 1, which attenuates IgE binding in sera of apple-allergic patients. Our results illustrate, from a structural perspective, the role that chemical modifications of allergens with components of the natural food matrix can play. Full article
(This article belongs to the Special Issue Structural Characterization of Food Proteins and Peptides)
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