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Functional Peptides: Processing Technology, Activity Evaluation and Application

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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 (30 November 2022) | Viewed by 6988

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Special Issue Editors

Dr. Shiyuan Dong

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Guest Editor

College of Food Science and Engineering, Ocean University of China, 5 Yushan Road, Qingdao 266003, China
Interests: functional foods; peptides; antioxidants; gut microbiota; in vitro digestion; antibacterial property; absorption; antihypertensive peptides; thermal processing method

Dr. Søren Drud-Heydary Nielsen

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Co-Guest Editor

Department of Food Science, Aarhus University, Blichers Allé 20, P.O. Box 50, DK-8830 Tjele, Denmark
Interests: proteomics; peptidomics; post-translational modifications; bioactivity; mass spectrometry; bioinformatics

Special Issue Information

Dear Colleagues,

The protein hydrolysates or peptides prepared from protein hydrolyzed with enzymes have multi-functional properties such as antioxidant activity, antibacterial properties and immunologic activity, and have received increasing attention as food ingredients or functional food in industry. Peptides have the same amino acid composition as homologous proteins, but also have better digestion and absorption performance than proteins, so they can maintain and improve the nutritional status of proteins. However, the targeting of most of peptides is poor and the functional activity of some peptides is low due to their purity. The interaction of peptides and carbohydrates, lipids and other compositions in food during thermal processing treatments is still most unknown when peptides are applied into a food system. The mechanism about absorption of some peptides from food protein hydrolysates is complex, and more works need to be further investigated.

Dr. Shiyuan Dong
Dr. Søren Drud-Heydary Nielsen
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

peptides
antioxidants
gut microbiota
in vitro digestion
antibacterial property
absorption
antihypertensive peptides
thermal processing method

Published Papers (3 papers)

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Research

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15 pages, 4755 KiB

Open AccessArticle

Formation of N^ε-Carboxymethyl-Lysine and N^ε-Carboxyethyl-Lysine in Heated Fish Myofibrillar Proteins with Glucose: Relationship with Its Protein Structural Characterization

by Siqi Zhang, Pengcheng Zhou, Peng Han, Hao Zhang, Shiyuan Dong and Mingyong Zeng

Foods 2023, 12(5), 1039; https://doi.org/10.3390/foods12051039 - 01 Mar 2023

Cited by 1 | Viewed by 1405

Abstract

The formation of advanced glycation end products (AGEs), including N^ε-carboxymethyl-lysine (CML) and N^ε-carboxyethyl-lysine (CEL), in a fish myofibrillar protein and glucose (MPG) model system at 80 °C and 98 °C for up to 45 min of heating were investigated. The characterization of protein structures, including their particle size, ζ-potential, total sulfhydryl (T-SH), surface hydrophobicity (H₀), sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) and Fourier transform infrared spectroscopy (FTIR), were also analyzed. It was found that the covalent binding of glucose and myofibrillar protein at 98 °C promoted protein aggregation when compared with the fish myofibrillar protein (MP) heated alone, and this aggregation was associated with the formation of disulfide bonds between myofibrillar proteins. Furthermore, the rapid increase of CEL level with the initial heating at 98 °C was related to the unfolding of fish myofibrillar protein caused by thermal treatment. Finally, correlation analysis indicated that the formation of CEL and CML had a significantly negative correlation with T-SH content (r = −0.68 and r = −0.86, p ≤ 0.011) and particle size (r = −0.87 and r = −0.67, p ≤ 0.012), but was weakly correlated with α-Helix, β-Sheet and H₀ (r² ≤ 0.28, p > 0.05) during thermal treatment. Overall, these findings provide new insights into the formation of AGEs in fish products based on changes of protein structure. Full article

(This article belongs to the Special Issue Functional Peptides: Processing Technology, Activity Evaluation and Application)

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15 pages, 2604 KiB

Open AccessArticle

Screening and Identification of Novel Soluble Epoxide Hydrolase Inhibitors from Corn Gluten Peptides

by Jiamin Dang, Shuangkui Du and Liying Wang

Foods 2022, 11(22), 3695; https://doi.org/10.3390/foods11223695 - 18 Nov 2022

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Abstract

The objective of this study was to investigate the soluble epoxide hydrolase (sEH) inhibitory properties of corn gluten peptides. In total, 400 dipeptides and 8000 tripeptides were first virtually screened by molecular docking and 30 potential sEH inhibitory peptides were selected. Among them, WEY, WWY, WYW, YFW, and YFY showed the highest sEH inhibitory activities with IC₅₀ values of 55.41 ± 1.55, 68.80 ± 7.72, 70.66 ± 9.90, 96.00 ± 7.5, and 94.06 ± 12.86 μM, respectively. These five peptides all behaved as mixed-type inhibitors and were predicted to form hydrogen bond interactions mainly with Asp333, a key residue located in the catalytic active site of sEH. Moreover, it was found that the corn gluten hydrolysates of Alcalase, Flavourzyme, pepsin and pancreatin all exhibited high sEH inhibitory activities, with IC₅₀ values of 1.07 ± 0.08, 1.19 ± 0.24, and 1.46 ± 0.31 mg/mL, respectively. In addition, the sEH inhibitory peptides WYW, YFW, and YFY were successfully identified from the corn gluten hydrolysates by Alcalase using nano-LC-MS/MS. This study demonstrated the sEH inhibitory capacity of peptides for the first time and corn gluten might be a promising food protein source for discovering novel natural sEH inhibitory peptides. Full article

(This article belongs to the Special Issue Functional Peptides: Processing Technology, Activity Evaluation and Application)

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Review

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27 pages, 2635 KiB

Open AccessReview

Enhancing the Biological Activities of Food Protein-Derived Peptides Using Non-Thermal Technologies: A Review

by Gbemisola J. Fadimu, Thao T. Le, Harsharn Gill, Asgar Farahnaky, Oladipupo Odunayo Olatunde and Tuyen Truong

Foods 2022, 11(13), 1823; https://doi.org/10.3390/foods11131823 - 21 Jun 2022

Cited by 14 | Viewed by 3636

Abstract

Bioactive peptides (BPs) derived from animal and plant proteins are important food functional ingredients with many promising health-promoting properties. In the food industry, enzymatic hydrolysis is the most common technique employed for the liberation of BPs from proteins in which conventional heat treatment is used as pre-treatment to enhance hydrolytic action. In recent years, application of non-thermal food processing technologies such as ultrasound (US), high-pressure processing (HPP), and pulsed electric field (PEF) as pre-treatment methods has gained considerable research attention owing to the enhancement in yield and bioactivity of resulting peptides. This review provides an overview of bioactivities of peptides obtained from animal and plant proteins and an insight into the impact of US, HPP, and PEF as non-thermal treatment prior to enzymolysis on the generation of food-derived BPs and resulting bioactivities. US, HPP, and PEF were reported to improve antioxidant, angiotensin-converting enzyme (ACE)-inhibitory, antimicrobial, and antidiabetic properties of the food-derived BPs. The primary modes of action are due to conformational changes of food proteins caused by US, HPP, and PEF, improving the susceptibility of proteins to protease cleavage and subsequent proteolysis. However, the use of other non-thermal techniques such as cold plasma, radiofrequency electric field, dense phase carbon dioxide, and oscillating magnetic fields has not been examined in the generation of BPs from food proteins. Full article

(This article belongs to the Special Issue Functional Peptides: Processing Technology, Activity Evaluation and Application)

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