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Functional Properties and Health Benefits of Bioactive Peptides Derived from...
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Functional Properties and Health Benefits of Bioactive Peptides Derived from Food

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Nutrition".

Deadline for manuscript submissions: closed (15 March 2023) | Viewed by 9565

Special Issue Editors

Prof. Dr. Bo Li

E-Mail Website
Guest Editor
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China
Interests: peptides; collagen; bioactive compounds; bioavailability; QSAR; antioxidant; anti-aging; anti-platelet
Dr. Hui Hong

E-Mail Website
Guest Editor
College of Food Science & Nutritional Engineering, China Agricultural University, Beijing, China
Interests: aquatic products; fish protein; peptides; quality control
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In recent years it has been recognized that dietary proteins provide a rich source of biologically active peptides. Such peptides are inactive within the sequence of the parent protein and can be released through hydrolysis by proteolytic enzymes or by proteolytic microorganisms (fermentation). Bioactive peptides derived from food have received increasing attention due to their health benefits in animal experiments and clinical trials. These beneficial effects include antioxidant, antimicrobial, anti-aging, anti-osteoporotic and anti-osteoarthritis, anti-inflammatory, regulation of the cardiovascular system (such as reduction of blood pressure, anti-thrombus), regulation of the immune system, etc. Protein hydrolysates are well acknowledged for their safety from a nutritional point of view, and there are some commercial protein products and ingredients with health or function claims based on bioactive peptides; however, what is the amino acid sequence of the bioactive peptides inside? What are the structure–activity relationships of the biopeptides? Their impact on the tissue or cell biology in vivo? Questions also remain regarding the bioavailability of bioactive peptides. All of these issues need to be further clarified. 

Prof. Dr. Bo Li
Dr. Hui Hong
Guest Editors

Manuscript Submission Information

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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
  • structure–activity relationship
  • bioavailability
  • protein hydrolysate
  • functional evaluation
  • health effect

Published Papers (5 papers)

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Research

14 pages, 3959 KiB  
Article
Silver Carp (Hypophthalmichthys molitrix) Scales Collagen Peptides (SCPs): Preparation, Whitening Activity Screening and Characterization
by Xiao-Yan Zu, Mei-Jin Li, Guang-Quan Xiong, Jun Cai, Tao Liao and Hai-Lan Li
Foods 2023, 12(7), 1552; https://doi.org/10.3390/foods12071552 - 06 Apr 2023
Cited by 2 | Viewed by 1775
Abstract
This study involves the preparation of scale collagen peptides (SCPs) with whitening activity from silver carp (Hypophthalmichthys molitrix) and their characterization and peptide sequence identification. In this article, scanning electron microscopy (SEM) was used to observe structure changes of sliver carp [...] Read more.
This study involves the preparation of scale collagen peptides (SCPs) with whitening activity from silver carp (Hypophthalmichthys molitrix) and their characterization and peptide sequence identification. In this article, scanning electron microscopy (SEM) was used to observe structure changes of sliver carp scales; enzymatic hydrolysis was optimized through protease screening and response surface optimization. The ultrafiltration was used to separate SCPs and the whitening activity was comprehensively evaluated using radical scavenging rate and tyrosinase-inhibiting activity, among others. An optimal component was characterized and identified using various modern spectral analysis techniques. The results showed that the surface of silver carp scales after decalcification was smooth and clear. The pepsin had the highest peptide yield and tyrosinase-inhibiting activity (90.01% and 82.25%, respectively). The optimal enzymatic hydrolysis conditions were an enzyme dosage of 16.1%, a solid–liquid ratio of 1:15.6 and a time of 4.9 h. The proportions of hydrophobic and basic amino acids in the peptide composition were 32.15% and 13.12%, respectively. Compared with SCPs2, SCPs1 (6096.68–9513.70 Da) showed better ·OH scavenging ability, tyrosinase-inhibiting activity and moisture absorption. SCPs1 was a macromolecular fragment of type I collagen with a triple helix structure, containing three peptide sequences with the potential for tyrosinase activity inhibition (AGPPGADGQTGQRGE, SGPAGIAGPAGPRGPAGPNGPPGKD and KRGSTGEQGSTGPLGMRGPRGAA). These results show that SCPs1 is a collagen peptide product with whitening potential. Full article
(This article belongs to the Special Issue Functional Properties and Health Benefits of Bioactive Peptides Derived from Food)
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12 pages, 2333 KiB  
Communication
Protective Effect of Glycomacropeptide on the Inflammatory Response of U937 Macrophages
by Laura Elena Córdova-Dávalos, Daniel Cervantes-García, Maria Fernanda Ballona-Alba, Alejandra Santos-López, Alma Saraí Esquivel-Basaldúa, Pamela Gallegos-Alcalá, Mariela Jiménez and Eva Salinas
Foods 2023, 12(7), 1528; https://doi.org/10.3390/foods12071528 - 04 Apr 2023
Cited by 1 | Viewed by 1659
Abstract
Macrophages play crucial roles in inflammation and oxidative stress associated with noncommunicable diseases, such as cardiovascular diseases, diabetes, and cancer. Glycomacropeptide (GMP) is a bioactive peptide derived from milk κ-casein that contains abundant sialic acid and has shown anti-inflammatory, antioxidative, anti-obesity, and anti-diabetic [...] Read more.
Macrophages play crucial roles in inflammation and oxidative stress associated with noncommunicable diseases, such as cardiovascular diseases, diabetes, and cancer. Glycomacropeptide (GMP) is a bioactive peptide derived from milk κ-casein that contains abundant sialic acid and has shown anti-inflammatory, antioxidative, anti-obesity, and anti-diabetic properties when is orally administered. The aim of this study was to evaluate the effect of GMP on the regulation of the inflammatory response in human macrophages and the participation of sialic acid in this activity. GMP pretreatment decreased by 35%, 35%, and 49% the production of nitrites, interleukin (IL)-1β, and tumor necrosis factor (TNF)-α, respectively, in activated human macrophages U937. The same effect was obtained when cells were pretreated with asialo GMP, and no change on the gene expression of the lectins associated with the recognition of sialic acids, SIGLEC5, 7, and 9, was induced by GMP on macrophages, which suggests that sialic acid might not be involved in this immunoregulatory effect. Interestingly, GMP increased 8.9- and 3.5-fold the gene expression of the canonical anti-inflammatory protein SOCS3 and the antioxidant enzyme HMOX1, respectively, in U937 cells. Thus, GMP exerts anti-inflammatory and antioxidative activities on activated macrophages in a sialic acid-independent manner, which might be related to its in vivo reported bioactivity. Full article
(This article belongs to the Special Issue Functional Properties and Health Benefits of Bioactive Peptides Derived from Food)
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13 pages, 2821 KiB  
Article
Structural Insights on Hyp-Gly-Containing Peptides as Antiplatelet Compounds through Topomer CoMFA and CoMSIA Analysis
by Yijie Yang, Qi Tian, Shiming Li and Bo Li
Foods 2023, 12(4), 777; https://doi.org/10.3390/foods12040777 - 10 Feb 2023
Cited by 1 | Viewed by 1108
Abstract
Increasing evidence has shown collagen hydrolysate involves a variety of bioactivities. In our previous study, multiple antiplatelet peptides containing Hyp/Pro-Gly were identified in collagen hydrolysates from Salmo salar and silver carp skin and exhibited anti-thrombosis activity without bleeding risks in vivo. However, the [...] Read more.
Increasing evidence has shown collagen hydrolysate involves a variety of bioactivities. In our previous study, multiple antiplatelet peptides containing Hyp/Pro-Gly were identified in collagen hydrolysates from Salmo salar and silver carp skin and exhibited anti-thrombosis activity without bleeding risks in vivo. However, the relationship between structure and activity remains unknown. We performed 3D-QSAR studies on 23 Hyp/Pro-Gly-containing peptides in which 13 peptides were reported before. CoMFA, Topomer CoMFA and CoMSIA analyses were used to generate the QSAR models. Topomer CoMFA analysis showed a q2 value of 0.710, an r2 value of 0.826, an r2pred value of 0.930, and the results showed that Hyp instead of Pro was more important for improving the antiplatelet activity. CoMSIA analysis showed a q2 value of 0.461, an r2 value of 0.999, and an r2pred value of 0.999. Compared with the electrostatic field and hydrogen bond donor field, the steric field, hydrophobic field and hydrogen bond receptor field have great influence on the activity of antiplatelet peptides. The predicted peptide EOGE exhibited antiplatelet activity induced by ADP, and inhibited thrombus formation (300 μmol/kg bw) without bleeding risks. Combined results of these studies indicate that OG-containing peptides had a potential to be developed into an effective specific medical food in the prevention of thrombotic diseases. Full article
(This article belongs to the Special Issue Functional Properties and Health Benefits of Bioactive Peptides Derived from Food)
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14 pages, 2681 KiB  
Article
Calcium Binding Mechanism of Soybean Peptide with Histidine Alteration by Molecular Docking Analysis and Spectroscopic Methods
by Jing Gan, Xiao Kong, Ziqun Xiao, Yuhang Chen, Mengdi Du, Yan Wang, Zhenhua Wang, Yongqiang Cheng and Bo Xu
Foods 2022, 11(20), 3290; https://doi.org/10.3390/foods11203290 - 20 Oct 2022
Cited by 2 | Viewed by 1547
Abstract
Histidine (His) carries a unique heteroaromatic imidazole side chain and plays an irreplaceable role in peptides and proteins. With the current study, we aimed to determine the characteristics and functional activities of the bone density of soy peptide–calcium complexes in which a His [...] Read more.
Histidine (His) carries a unique heteroaromatic imidazole side chain and plays an irreplaceable role in peptides and proteins. With the current study, we aimed to determine the characteristics and functional activities of the bone density of soy peptide–calcium complexes in which a His residue was replaced by Leu (CBP-H). Soybean peptide (CBP-H) was chemically synthesized, the binding mechanism between CBP-H and calcium ions in combination was determined with bioinformatics and spectroscopy analysis, and the difference between CBP and CBP-H was investigated. Finally, we analyzed the effect of CBP and CBP-H on osteoblasts in vitro. The results showed that CBP-H could bind to calcium ions, and the calcium coordinated with the carboxyl groups of Asp and Glu in the peptide. The nitrogen atoms of the amino group and the oxygen atoms of the carboxyl group in CBP-H significantly contributed to the coordination with Ca2+. Furthermore, the binding capacity was 36.48 ± 0.09 mg/g, similar to CBP. However, both CBP and CBP-H could promote osteogenic activity, the activity of CBP-H was 127.147%, lower than CBP (121.777%). While it had the same ability to promote intracellular calcium concentration, CBP-H could upregulate 150.12% calcium ions into the intracellular, and the rate of the rise of CBP was 158.91%, further highlighting the potential of His residues for binding calcium and treating osteoporosis. Full article
(This article belongs to the Special Issue Functional Properties and Health Benefits of Bioactive Peptides Derived from Food)
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10 pages, 2164 KiB  
Article
Soft-Shelled Turtle Peptide Supplementation Modifies Energy Metabolism and Oxidative Stress, Enhances Exercise Endurance, and Decreases Physical Fatigue in Mice
by Hao Zhong, Jinyuan Shi, Junhui Zhang, Qianqian Wang, Yipeng Zhang, Peng Yu, Rongfa Guan and Fengqin Feng
Foods 2022, 11(4), 600; https://doi.org/10.3390/foods11040600 - 19 Feb 2022
Cited by 10 | Viewed by 2661
Abstract
The potential of soft-shelled turtle peptides (STP) against fatigue was evaluated. Mice orally supplemented with STP significantly increased the swimming time until tiredness by 35.4–57.1%. Although not statistically significant, STP increased muscle and thymus mass. In addition, the serum lactate, ammonia, blood urea [...] Read more.
The potential of soft-shelled turtle peptides (STP) against fatigue was evaluated. Mice orally supplemented with STP significantly increased the swimming time until tiredness by 35.4–57.1%. Although not statistically significant, STP increased muscle and thymus mass. In addition, the serum lactate, ammonia, blood urea nitrogen content and creatine kinase activity in STP-fed mice were dramatically decreased when compared to the control group. Furthermore, STP supplementation increased the reserves of liver glycogen and muscle glycogen, thus improved the energy metabolism system of mice. STP treatment contributed to increased superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities as well as a decrease in malondialdehyde (MDA), indicating an improvement in oxidative stress protection. The Western blot (WB) results indicated that the STP supplement effectively altered the expression of oxidative stress-related protein by modulating the NRF2/KEAP1 pathway. In summary, STP affected NRF2/KEAP1 levels in skeletal muscle, leading to antioxidant activity and a slower time to exhaustion during exercise. Full article
(This article belongs to the Special Issue Functional Properties and Health Benefits of Bioactive Peptides Derived from Food)
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