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Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and...
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Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition

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

Deadline for manuscript submissions: closed (31 October 2024) | Viewed by 8025

Special Issue Editors

Dr. Maolin Tu

E-Mail Website
Guest Editor
College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, China
Interests: bioactive peptides; protein; bioinformatics; bioavailability; microcapsules; gut microbiota; probiotics
Prof. Dr. Yali Dang

E-Mail Website
Guest Editor
College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, China
Interests: bioactive peptides; protein; umami peptide
Dr. Jiarun Han

E-Mail Website
Guest Editor
School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310058, China
Interests: antimicrobial peptides; marine proteins; bioavailability

Special Issue Information

Dear Colleagues,

Food-derived proteins and peptides not only serve as a fundamental nutrients for humans but also provide some properties that promote human health, meaning that they can have important roles during food processing based on their specific biochemistry characteristics. This Special Issue welcomes studies focusing on the following topics: (1) the activity and bioavailability of food-derived peptides and proteins, (2) the emerging technologies used in the research of peptides and proteins, (3) the application of peptides and proteins in food industries, (4) the exploration of novel sources regarding bioactive peptide and proteins, (5) the rapid screening and detection of biopeptides and proteins. This Special Issue will provide an overview of the advancements in this field and present research conducted on food-derived proteins and peptides intended for use in the food industries.

Dr. Maolin Tu
Prof. Dr. Yali Dang
Dr. Jiarun Han
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

  • bioactive peptides
  • bioactive proteins
  • structure
  • active mechanisms
  • nutrition and function
  • bioavailability

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Published Papers (6 papers)

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Research

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14 pages, 1993 KiB  
Article
Physicochemical and Antioxidative Properties of Protein Hydrolysates from Residual Goat Placenta Extract by Two Different Methods
by Yinchen Hou, Xinyang Chen, Qihui Shi, Mingyi Zhang, Shengru Yang, Long Pan, Quanping Liu, Yongchao Fan, Rongchao Qiu and Aimei Liao
Foods 2024, 13(20), 3263; https://doi.org/10.3390/foods13203263 - 14 Oct 2024
Viewed by 981
Abstract
Protein hydrolysates from the goat placenta provide multiple benefits, such as immune system enhancement, antioxidant activities, and reductions in uric acid levels. Despite these benefits, their industrial applications have been underexplored. This study aimed to prepare extract protein hydrolysates (GPERPs) from residual goat [...] Read more.
Protein hydrolysates from the goat placenta provide multiple benefits, such as immune system enhancement, antioxidant activities, and reductions in uric acid levels. Despite these benefits, their industrial applications have been underexplored. This study aimed to prepare extract protein hydrolysates (GPERPs) from residual goat placenta extract (GPER) and assess their functional properties, focusing on how different drying methods influence these properties. The essential amino acid contents were 30.94% for the GPER and 34.11% for the GPERPs. Moreover, all the essential amino acids were present, and the amino acid score (AAS) for each exceeded 1.0 in the GPERPs. The foaming properties of the spray-dried GPERPs (95.56 ± 5.89%) were significantly greater than those of the freeze-dried GPERPs (49.13 ± 4.17%) at pH values of 4.0~10.0. The emulsion stability (ES) of the spray-dried GPERPs (453.44 ± 8.13 min) was notably greater than that of the freeze-dried GPERPs (245.58 ± 7.12 min). Furthermore, the water retention capacity (WRC) of the freeze-dried GPERPs (201.49 ± 6.12%) was significantly greater than that of the spray-dried GPERPs (103.35 ± 7.13%), except at pH 10.0 (101.44 ± 8.13%). Similarly, at pH values of 6.0, 8.0, and 10.0, the oil retention capacity (ORC) of the freeze-dried GPERPs (715.58 ± 12.15%) was significantly greater than that of the spray-dried GPERPs (560.56 ± 11.15%), although the opposite trend was noted under acidic conditions. In terms of the antioxidant activity, the ability of the goat placenta extract residual protein hydrolysates (GPERPs) to scavenge DPPH radicals and superoxide anion radicals increased with the increasing peptide powder concentration, and the maximum scavenging rates of the DPPH radicals (39.5 ± 0.56%) and superoxide anions (81.2 ± 0.54%) in the freeze-dried peptide powder were greater than those in the spray-dried peptide powder. These findings contribute to the understanding of the physicochemical and antioxidant properties of GPERPs under various drying methods and provide fundamental data for the development of functional foods based on GPERPs. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition)
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17 pages, 2028 KiB  
Article
Cryoprotective Activity of Different Characterized Fractions Isolated from Enzymatic Hydrolysates of Croceine Croaker (Pseudosciaena crocea)
by Zhe Xu, ShengAo Cao, Na Cui, Rui Zhang, Shuang Zhao, Lijuan Zhang, Shuang Guan, Yikun Xu, Xu Yan, Zhixuan Zhu, Zhijian Tan and Tingting Li
Foods 2024, 13(12), 1946; https://doi.org/10.3390/foods13121946 - 20 Jun 2024
Viewed by 998
Abstract
In this study, ultrafiltration fractions (<3 k Da, LMH; >3 k Da, HMH) and solid-phase extraction fractions (hydrophilic hydrolysate, HIH; hydrophobic hydrolysate, HOH) from trypsin hydrolysate purified from croceine croaker (Pseudosciaena crocea) isolate were obtained to investigate the cryoprotective effects of [...] Read more.
In this study, ultrafiltration fractions (<3 k Da, LMH; >3 k Da, HMH) and solid-phase extraction fractions (hydrophilic hydrolysate, HIH; hydrophobic hydrolysate, HOH) from trypsin hydrolysate purified from croceine croaker (Pseudosciaena crocea) isolate were obtained to investigate the cryoprotective effects of the different fractions, achieved by means of maceration of turbot fish meat after three freeze-thaw cycles. Alterations in the texture, color, moisture loss, myofibrillar protein oxidation stability and conformation, and microstructure of the fish were analyzed after freezing and thawing. The results demonstrate that HIH maximized the retention of fish texture, reduced moisture loss, minimized the oxidation and aggregation of myofibrillar proteins, and stabilized the secondary and tertiary structures of myofibrillar proteins compared to the control group. In conclusion, the HIH component in the trypsin hydrolysates of croceine croaker significantly contributes to minimizing freeze damage in fish meat and acts as an anti-freezing agent with high industrial application potential. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition)
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13 pages, 2084 KiB  
Article
Preparation of Calcium–Binding Peptides Derived from Mackerel (Scomber japonicus) Protein and Structural Characterization and Stability Analysis of Its Calcium Complexes
by Pengbo Cui, Jianqin Liang, Tianyu Cheng and Jianyou Zhang
Foods 2024, 13(11), 1652; https://doi.org/10.3390/foods13111652 - 25 May 2024
Cited by 2 | Viewed by 997
Abstract
The purpose of this study was to prepare mackerel peptides (MPs) with calcium-binding capacity through an enzyme method and to investigate the potential role they play in improving the bioavailability of calcium in vitro. The calcium-binding capacity, degree of hydrolysis (DH), molecular weight [...] Read more.
The purpose of this study was to prepare mackerel peptides (MPs) with calcium-binding capacity through an enzyme method and to investigate the potential role they play in improving the bioavailability of calcium in vitro. The calcium-binding capacity, degree of hydrolysis (DH), molecular weight (MW), and charge distribution changes with the enzymolysis time of MPs were measured. The structural characterization of mackerel peptide–calcium (MP–calcium) complexes was performed using spectroscopy and morphology analysis. The results showed that the maximum calcium-binding capacity of the obtained MPs was 120.95 mg/g when alcalase was used for 3 h, with a DH of 15.45%. Moreover, with an increase in hydrolysis time, the MW of the MPs decreased, and the negative charge increased. The carboxyl and amino groups in aspartic (Asp) and glutamate (Glu) of the MPs may act as calcium-binding sites, which are further assembled into compact nanoscale spherical complexes with calcium ions through intermolecular interactions. Furthermore, even under the influence of oxalic acid, MP–calcium complexes maintained a certain solubility. This study provides a basis for developing new calcium supplements and efficiently utilizing the mackerel protein resource. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition)
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17 pages, 732 KiB  
Article
Investigating the Nutritional and Functional Properties of Protaetia brevitarsis Larvae and Isolated Soy Protein Mixtures as Alternative Protein Sources
by Eun-Chae Cho, Surin Ahn, Hyo-Jeong Hwang, Kyung-Ok Shin, Suwan Kim and Yean-Jung Choi
Foods 2024, 13(10), 1540; https://doi.org/10.3390/foods13101540 - 15 May 2024
Viewed by 1557
Abstract
The growing demand for sustainable and alternative protein sources has spurred interest in insect-based and plant-based proteins. Protaetia brevitarsis (PB) larvae and isolated soy protein (ISP) are notable in this regard, offering potential health benefits and nutritional enhancements. We assessed the feasibility of [...] Read more.
The growing demand for sustainable and alternative protein sources has spurred interest in insect-based and plant-based proteins. Protaetia brevitarsis (PB) larvae and isolated soy protein (ISP) are notable in this regard, offering potential health benefits and nutritional enhancements. We assessed the feasibility of PB larvae and ISP mixtures as alternative food ingredients. Methods included the optimized purification and freeze-drying of PB larvae, extraction and refinement of legume proteins, physicochemical and antioxidant capacity evaluations, DPPH radical scavenging activity measurement, total phenolic and flavonoids content quantification, general component analysis, amino acid profiling using HPLC, fatty acid profiling through gas chromatography, and mineral content analysis using inductively coupled plasma spectrometry. The study found that certain PB:ISP ratios, particularly a 7:3 ratio, significantly improved the blend’s antioxidant capacity, as evidenced by DPPH scavenging activity. This ratio also impacted the nutritional profile by altering the mixture’s general components, with a notable increase in moisture, crude protein, and fiber and a decrease in crude fat and ash. Amino acid analysis revealed a balanced presence of essential and non-essential amino acids. The fatty acid profile was rich in unsaturated fatty acids, especially in certain ratios. Mineral analysis showed a complex interplay between PB larvae and ISP, with some minerals decreasing and others increasing in the blend. PB larvae and ISP mixtures have significant potential as alternative protein sources, offering a diversified nutritional profile and enhanced antioxidant properties. The 7:3 ratio of PB larvae to ISP has been shown to be particularly effective, suggesting that this ratio may offer an optimal balance for enhancing the overall nutritional quality of the mixture. This study sets the stage for future research to further explore and optimize the potential of these mixtures for human consumption while considering the challenges of consumer acceptance and long-term safety. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition)
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14 pages, 2207 KiB  
Article
Zein-Derived Peptides from Corn Promote the Proliferation of C2C12 Myoblasts via Crosstalk of mTORC1 and mTORC2 Signaling Pathways
by Mohammad Sadiq Amin, Binbin Yu, Dongjing Wu, Yujia Lu, Wei Wu, Jing Wang, Yuhao Zhang and Yu Fu
Foods 2024, 13(6), 919; https://doi.org/10.3390/foods13060919 - 18 Mar 2024
Cited by 1 | Viewed by 2159
Abstract
Dietary protein supplementation has emerged as a promising strategy in combating sarcopenia. Furthermore, searching for alternatives of animal proteins has been a hot topic. The present study aimed to investigate the effects of zein peptides on C2C12 myoblasts and explore [...] Read more.
Dietary protein supplementation has emerged as a promising strategy in combating sarcopenia. Furthermore, searching for alternatives of animal proteins has been a hot topic. The present study aimed to investigate the effects of zein peptides on C2C12 myoblasts and explore their potential molecular mechanisms. The proliferative, cell cycle, and anti-apoptotic activities of zein peptides were evaluated. Peptidomics analysis and transcriptome sequencing were employed to explore the structure-activity relationship and underlying molecular mechanisms. The results indicated that zein peptides (0.05–0.2 mg/mL) exerted a significant proliferation-promoting impact on C2C12 cells, via increasing cell viability by 33.37 to 42.39%. Furthermore, zein peptides significantly increased S phase proportion and decreased the apoptosis rate from 34.08% (model group) to 28.96% in C2C12 cells. In addition, zein peptides exhibited a pronounced anti-apoptotic effect on C2C12 cells. Zein peptides are abundant in branch-chain amino acids, especially leucine. Transcriptomics analysis revealed that zein peptides can promote proliferation, accelerate cell cycle, and improve protein synthesis of muscle cells through mTORC1 and mTORC2 signaling pathways. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition)
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Review

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16 pages, 5060 KiB  
Review
Investigating the Role of Food-Derived Peptides in Hyperuricemia: From Mechanisms of Action to Structural Effects
by Yu Han, Wanlu Liu, Kexin Li, Mingzhen Zhang, Xinqi Liu, Lu Li, Zhao Guo and He Li
Foods 2025, 14(1), 58; https://doi.org/10.3390/foods14010058 - 28 Dec 2024
Viewed by 472
Abstract
Hyperuricemia, a disorder of purine metabolism associated with cardiovascular disease, gout, and kidney disease, can be alleviated by food-derived peptides. However, the precise mechanisms remain unclear, hindering their development. This study reviews uric acid-lowering peptides from various sources, focusing on two pathways: inhibiting [...] Read more.
Hyperuricemia, a disorder of purine metabolism associated with cardiovascular disease, gout, and kidney disease, can be alleviated by food-derived peptides. However, the precise mechanisms remain unclear, hindering their development. This study reviews uric acid-lowering peptides from various sources, focusing on two pathways: inhibiting uric acid production and promoting excretion. Low-molecular-weight peptides (<1000 Da) exhibited superior uric acid-lowering effects. We further explored the relationships between amino acid composition and their target interactions. Peptides rich in cyclic amino acids (tryptophan, phenylalanine, and histidine) and containing small amounts of linear amino acids (leucine, cysteine, and glycine) demonstrated significant potential for lowering uric acid. These findings provide theoretical support for developing novel functional foods for the management of hyperuricemia. Full article
(This article belongs to the Special Issue Bioactive Proteins and Peptides Derived from Foods: Biochemistry, Functionality and Nutrition)
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