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Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg)

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A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Nutraceuticals, Functional Foods, and Novel Foods".

Deadline for manuscript submissions: closed (20 October 2021) | Viewed by 19035

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Special Issue Editors

Prof. Dr. Barbara Wróblewska

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Guest Editor

Institute of Animal Reproduction and Food Research, PAN, Olsztyn, Poland
Interests: food allergy; cow’s milk protein hypersensitivity; mucosal immunity; gut intestinal microbiota; modified diet; food digestion; food technology
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Małgorzata Darewicz

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Guest Editor

University of Warmia and Mazury in Olsztyn, Faculty of Food Science, Poland
Interests: proteins; peptides; antioxidants; food technology; food quality and safety; human nutrition; functional food; diet-related diseases

Prof. Dr. Jerzy Juśkiewicz

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Guest Editor

Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, 10 Tuwima Street, 10-718 Olsztyn, Poland
Interests: gut microbiota activity; metabolism; in vivo experiments; nutrition; oxidative stress; inflammation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food is a rich matrix of bioactive compounds with beneficial properties, yet it is also a cocktail of dangerous allergens. Development in the understanding of the influence of bioactive proteins and peptides on the human organism has now become the core of many studies. Novel food sources and food processing technologies are a potential sources of unknown bioactive peptides and new allergens. The diversity of food compounds’ activities and interactions with the host causes immunomodulation in organisms. These immune mechanisms are investigated at various levels, including cellular, tissue, and cohort. Knowledge about them will allow the development of new therapies and/or prophylaxis in the field of inflammation, allergies, and other non-communicable diseases.

We would like to invite experts from the areas of food allergy, food technology, food safety, bioinformatics, and similar fields to contribute to this Foods Special Issue that will be devoted to the topics described above. We expect original articles, reviews, and short communications, which will help to consolidate the current state-of-the-art knowledge.

Prof. Dr. Barbara Wróblewska
Prof. Dr. Małgorzata Darewicz
Prof. Dr. Jerzy Juśkiewicz
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

food-derived bioactive proteins and peptides
food allergenicity
novel food allergens
food processing
host immune modulation
functional food
personalized food
immune mechanism of bioactive compounds
in silico prediction
bioinformatics

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Published Papers (6 papers)

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Research

18 pages, 1743 KiB

Open AccessArticle

Mapping B-Cell Epitopes for Nonspecific Lipid Transfer Proteins of Legumes Consumed in India and Identification of Critical Residues Responsible for IgE Binding

by Ankita Mishra and Ashok Kumar

Foods 2021, 10(6), 1269; https://doi.org/10.3390/foods10061269 - 2 Jun 2021

Cited by 2 | Viewed by 2490

Abstract

Nonspecific lipid transfer proteins (nsLTPs) have been categorized as panallergens and display widespread occurrence across plant-kingdom. Present study, investigated B-cell epitopes for LTPs from chickpea, mung-bean, cowpea, pigeon-pea, and soybean via in silico methods. In-silico predicted regions were evaluated for epitope-conservancy and property-based peptide similarity search by different allergen databases. Additionally, the in-silico predicted regions were compared with the experimentally validated epitopes of peach-LTP. Sequence-homology studies showed that chickpea and mung-bean LTPs shared significant homology, i.e., >70% and >60%, respectively, with other LTP allergens from lentil, garden-pea, peanut, etc. Phylogenetic-analysis also showed chickpea and mung-bean LTPs to be closely related to allergenic LTPs from lentil and peanut, respectively. Epitope-conservation analysis showed that two of the predicted B-cell epitopic regions in chickpea and mung-bean LTPs were also conserved in other allergenic LTPs from peach, peanut, garden-pea, lentil, and green-bean, and might serve as conserved B-cell epitopes of the LTP protein family. Property-distance index values for chickpea and mung-bean LTPs also showed that most of the epitopes shared similarity with the reported allergens like-lentil, peanut, apple, plum, tomato, etc. Present findings, may be explored for identification of probable allergenicity of novel LTPs, on the basis of the reported conserved B-cell epitopes, responsible for potential cross-reactivity. Full article

(This article belongs to the Special Issue Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg))

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15 pages, 3022 KiB

Open AccessArticle

A Comparative Analysis of Novel Deep Learning and Ensemble Learning Models to Predict the Allergenicity of Food Proteins

by Liyang Wang, Dantong Niu, Xinjie Zhao, Xiaoya Wang, Mengzhen Hao and Huilian Che

Foods 2021, 10(4), 809; https://doi.org/10.3390/foods10040809 - 9 Apr 2021

Cited by 21 | Viewed by 3971

Abstract

Traditional food allergen identification mainly relies on in vivo and in vitro experiments, which often needs a long period and high cost. The artificial intelligence (AI)-driven rapid food allergen identification method has solved the above mentioned some drawbacks and is becoming an efficient auxiliary tool. Aiming to overcome the limitations of lower accuracy of traditional machine learning models in predicting the allergenicity of food proteins, this work proposed to introduce deep learning model—transformer with self-attention mechanism, ensemble learning models (representative as Light Gradient Boosting Machine (LightGBM) eXtreme Gradient Boosting (XGBoost)) to solve the problem. In order to highlight the superiority of the proposed novel method, the study also selected various commonly used machine learning models as the baseline classifiers. The results of 5-fold cross-validation showed that the area under the receiver operating characteristic curve (AUC) of the deep model was the highest (0.9578), which was better than the ensemble learning and baseline algorithms. But the deep model need to be pre-trained, and the training time is the longest. By comparing the characteristics of the transformer model and boosting models, it can be analyzed that, each model has its own advantage, which provides novel clues and inspiration for the rapid prediction of food allergens in the future. Full article

(This article belongs to the Special Issue Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg))

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23 pages, 1129 KiB

Open AccessArticle

Two Faces of Milk Proteins Peptides with Both Allergenic and Multidimensional Health Beneficial Impact—Integrated In Vitro/In Silico Approach

by Anna Maria Ogrodowczyk, Ivan Dimitrov and Barbara Wróblewska

Foods 2021, 10(1), 163; https://doi.org/10.3390/foods10010163 - 14 Jan 2021

Cited by 6 | Viewed by 2671

Abstract

The main food-origin antigens that the infant’s body is in contact with are cow’s milk proteins (CMP). Still, CMP are one of the main sources of beneficial biologically active peptides that play a role in treatment of non-communicable diseases. Safe methods to quickly predict the sensitizing potential of food proteins among their range of health-promoting properties are essential. The aim of study was to adapt an integrated approach combining several in silico (IS) studies and in vitro (IV) assays to screen the multifunctionality of CMP-derived peptides. Major histocompatability complex type II MHC II-binders, interleukin-4 and -10 inducers, interferon γ -inducers and immunobioactivity tools were used to predict the peptide-power of inducing allergies or tolerance. A comparison of the peptide profiless revealed the presence of one identical and one overlapping sequence in IS and IV hydrolysate. By IS analysis, four of 24 peptides were found to have high affinity and stimulate IL-4 expression, and by IV, one of seven peptides had this potential (Bos d9 peptide DIPNPIGSENSEK (195–208)). Three IV peptides may induce IL-10 expression. The IV/IS assessment seems promising agents for peptides’ potential determination dedicated only to preliminary screening of peptides. The IV verification is still crucial in further steps of studies. Full article

(This article belongs to the Special Issue Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg))

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12 pages, 1838 KiB

Open AccessArticle

Thaumatin-Like Protein (Pru av 2) Is a Cherry Allergen That Triggers Percutaneous Sensitization in Mice

by Eri Izumi, Shota Hidaka, Ayako Hiroi, Serina Kinugasa, Erika Yano, Nobuhiro Zaima and Tatsuya Moriyama

Foods 2021, 10(1), 134; https://doi.org/10.3390/foods10010134 - 10 Jan 2021

Cited by 9 | Viewed by 2770

Abstract

Numerous recent studies have suggested that food allergens enter the skin and predispose individuals to food allergies through the production of IgE antibodies in the body. Cherries are a popular fruit eaten worldwide. However, cherries are an allergenic food and percutaneous sensitization with cherry allergens through the perioral region may occur while ingesting cherries. The identity of the cherry protein that triggers percutaneous sensitization in humans or animal models remains unknown. In this study, the backs of BALB/c mice were shaved and crude cherry extracts containing sodium dodecyl sulfate were applied to the skin. Thereafter, the cherry-specific IgE and IgG1 antibodies generated and secreted in response to the epidermal application were measured using an enzyme-linked immunosorbent assay or immunoblotting. Skin exposure to cherry extracts elevated cherry-specific IgG1 levels. Application of fractionated and purified cherry proteins (antigen candidates for percutaneous sensitization) that bound to the IgG1 antibodies led to the identification of a thaumatin-like protein (Pru av 2). This molecule is known as the major cherry allergen that affects humans. In conclusion, our study identified Pru av 2 as a cherry allergen that triggers percutaneous sensitization in mice for the first time. Full article

(This article belongs to the Special Issue Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg))

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14 pages, 3237 KiB

Open AccessArticle

Exploring Potential Bioactive Peptides in Fermented Bactrian Camel’s Milk and Mare’s Milk Made by Mongolian Nomads

by Khuukhenbaatar Ganzorig, Tadasu Urashima and Kenji Fukuda

Foods 2020, 9(12), 1817; https://doi.org/10.3390/foods9121817 - 7 Dec 2020

Cited by 15 | Viewed by 3097

Abstract

To date, bioactive proteins and peptides from minor livestock milks and their fermented products have been scarcely reported. In Mongolia, nomads are commonly rearing five livestock animal species (i.e., cow, camel, goat, horse, and sheep) for milking and other purposes. In this study, we analyzed the peptide composition in fermented milks of Bactrian camels (Camelus bactrianus) and horses, produced by Mongolian nomads for self-consumption. Peptides from skimmed fermented milks were separated by ultrafiltration and reverse-phase high-performance liquid chromatography. Then, their amino acid sequences were determined by matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. Consequently, eleven peptides were identified in the fermented camel’s milk including four from β-casein (β-CN), three from α_s1-CN, and two from both κ-CN and lactophorin. On the other hand, twenty-four peptides were identified in the fermented mare’s milk including nineteen from β-CN, three from α_s1-CN, and one from both κ-CN and α_s2-CN. According to previous reports on the bioactivities of milk-derived peptides, antibacterial and antihypertensive activities were promising in both the fermented camel’s milk and mare’s milk. In addition, potential antioxidant activity was conjectured in the fermented camel’s milk. Further investigations are currently needed to clarify the potential role of immunomodulatory peptides in the two fermented milks. Full article

(This article belongs to the Special Issue Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg))

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13 pages, 2406 KiB

Open AccessArticle

Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation

by Jelena Radosavljević, Danijela Apostolović, Jelena Mihailović, Marina Atanasković-Marković, Lidija Burazer, Marianne van Hage and Tanja Ćirković Veličković

Foods 2020, 9(11), 1576; https://doi.org/10.3390/foods9111576 - 30 Oct 2020

Cited by 13 | Viewed by 3144

Abstract

The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow’s milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow’s milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 ± 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation. Full article

(This article belongs to the Special Issue Advances in the Bioactivity and Allergenicity of Food Proteins and Peptides (BioAllerg))

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