Discovery, Functions and Applications of Food-Derived Bioactive Peptides

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

Deadline for manuscript submissions: 30 November 2024 | Viewed by 2894

Special Issue Editor


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Guest Editor
Bioengineering College, Chongqing University, Chongqing, China
Interests: development of functional foods; discovery of bioactive peptide; design of natural inhibitors; antioxidants; molecular interaction of functional factors
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Special Issue Information

Dear Colleague,

With the increasing interest in food components, bioactive peptides have garnered significant attention since these peptides, derived from various food sources, exhibit diverse physiological functions including antioxidant, antimicrobial, blood pressure-lowering, and immunomodulatory activities, etc. This Special Issue focuses on (i) the discovery methods and processes of these peptides, involving wet-experiments and dry-experiments; (ii) their functions and mechanisms of action in health and disease management; and (iii) their potential applications in the food industry and medicine. Our aim is to enhance our understanding of these peptides and explore their practical utilization across various domains. Readers can expect a comprehensive overview of the latest research advancements in this field, paving the way for future developments and applications of food-derived bioactive peptides.

Prof. Dr. Guizhao Liang
Guest Editor

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Keywords

  • bioactive peptides
  • structure–activity relationships
  • artificial intelligence
  • peptide design
  • virtual screening
  • physiological function
  • interaction mechanisms

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Published Papers (3 papers)

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Research

14 pages, 4524 KiB  
Article
Sequence–Activity Relationship of Angiotensin-Converting Enzyme Inhibitory Peptides Derived from Food Proteins, Based on a New Deep Learning Model
by Dongya Qin, Xiao Liang, Linna Jiao, Ruihong Wang, Yi Zhao, Wenjun Xue, Jinhong Wang and Guizhao Liang
Foods 2024, 13(22), 3550; https://doi.org/10.3390/foods13223550 - 7 Nov 2024
Viewed by 662
Abstract
Food-derived peptides are usually safe natural drug candidates that can potentially inhibit the angiotensin-converting enzyme (ACE). The wet experiments used to identify ACE inhibitory peptides (ACEiPs) are time-consuming and costly, making it important and urgent to reduce the scope of experimental validation through [...] Read more.
Food-derived peptides are usually safe natural drug candidates that can potentially inhibit the angiotensin-converting enzyme (ACE). The wet experiments used to identify ACE inhibitory peptides (ACEiPs) are time-consuming and costly, making it important and urgent to reduce the scope of experimental validation through bioinformatics methods. Here, we construct an ACE inhibitory peptide predictor (ACEiPP) using optimized amino acid descriptors (AADs) and long- and short-term memory neural networks. Our results show that combined-AAD models exhibit more efficient feature transformation ability than single-AAD models, especially the training model with the optimal descriptors as the feature inputs, which exhibits the highest predictive ability in the independent test (Acc = 0.9479 and AUC = 0.9876), with a significant performance improvement compared to the existing three predictors. The model can effectively characterize the structure–activity relationship of ACEiPs. By combining the model with database mining, we used ACEiPP to screen four ACEiPs with multiple reported functions. We also used ACEiPP to predict peptides from 21,249 food-derived proteins in the Database of Food-derived Bioactive Peptides (DFBP) and construct a library of potential ACEiPs to facilitate the discovery of new anti-ACE peptides. Full article
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18 pages, 1470 KiB  
Article
Evaluation of Prebiotic and Health-Promoting Functions of Honeybee Brood Biopeptides and Their Maillard Reaction Conjugates
by Sakaewan Ounjaijean, Supakit Chaipoot, Rewat Phongphisutthinant, Gochakorn Kanthakat, Sirinya Taya, Pattavara Pathomrungsiyounggul, Pairote Wiriyacharee and Kongsak Boonyapranai
Foods 2024, 13(17), 2847; https://doi.org/10.3390/foods13172847 - 7 Sep 2024
Viewed by 800
Abstract
This study addresses the growing interest in natural functional ingredients by evaluating the prebiotic and health-promoting functions of honeybee brood biopeptides (HBb-Bps) and their conjugates. The purpose was to investigate their antioxidant activities, enzyme inhibition properties, and effects on probiotic growth and short-chain [...] Read more.
This study addresses the growing interest in natural functional ingredients by evaluating the prebiotic and health-promoting functions of honeybee brood biopeptides (HBb-Bps) and their conjugates. The purpose was to investigate their antioxidant activities, enzyme inhibition properties, and effects on probiotic growth and short-chain fatty acid (SCFA) production. The HBb-Bps were conjugated with honey, glucose, and fructose via the Maillard reaction. Antioxidant activities were assessed using DPPH and ABTS assays. The inhibitory effects on amylase, pancreatic lipase, and the angiotensin-converting enzyme (ACE) were measured. Probiotic growth and SCFA production were evaluated using L. plantarum TISTR846, and L. lactis TISTR1464. The HBb-Bps and their conjugates exhibited enhanced antioxidant activities post-Maillard reaction. They showed moderate enzyme inhibition, which decreased after conjugation. However, ACE inhibition increased with conjugation. The HBb-Bps significantly promoted probiotic growth and SCFA production, with further enhancement by the Maillard reaction. Overall, the HBb-Bps and their conjugates demonstrate significant prebiotic and health-promoting functions, suggesting their potential as natural ingredients in functional foods and nutraceuticals. Further research should focus on the in vivo effects and, given their solubility and stability these biopeptides could be incorporated into functional food formulations, such as health beverages, protein bars, and other fortified foods designed to deliver specific health benefits. Full article
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19 pages, 2920 KiB  
Article
Biocontrol Strategy of Listeria monocytogenes in Ready-to-Eat Pork Cooked Ham Using Peptic Hydrolysates of Porcine Hemoglobin
by Zain Sanchez-Reinoso, Sarah Todeschini, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet and Sergey Mikhaylin
Foods 2024, 13(15), 2394; https://doi.org/10.3390/foods13152394 - 29 Jul 2024
Viewed by 1060
Abstract
Listeria monocytogenes is a foodborne pathogen that represents a serious concern for ready-to-eat (RTE) meat products due to its persistence in production facilities. Among the different strategies for the control of this pathogen, the use of antimicrobial peptides derived from food by-products, such [...] Read more.
Listeria monocytogenes is a foodborne pathogen that represents a serious concern for ready-to-eat (RTE) meat products due to its persistence in production facilities. Among the different strategies for the control of this pathogen, the use of antimicrobial peptides derived from food by-products, such as slaughterhouse blood proteins, has emerged as a promising biocontrol strategy. This study evaluated for the first time the use of peptic hydrolysates of porcine hemoglobin as a biocontrol strategy of L. monocytogenes in RTE pork cooked ham. Pure porcine hemoglobin (Hb-P) and porcine cruor (P-Cru) were hydrolyzed using pepsin at different temperatures (37 °C for Hb-P and 23 °C for P-Cru) for 3 h. Then, the hydrolysates were characterized in terms of their degree of hydrolysis (DH), peptide population, color, and antimicrobial activity (in vitro and in situ) against three different serotypes of L. monocytogenes. Reducing the hydrolysis temperature of P-Cru by 14 °C resulted in a 2 percentage unit decrease in DH and some differences in the peptide composition. Nevertheless, the antimicrobial activity (in situ) was not significantly impacted, decreasing the viable count of L. monocytogenes by ~1-log and retarding their growth for 21 days at 4 °C. Although the color of the product was visibly altered, leading to more saturated reddish and yellowish tones and reduced brightness, the discoloration of the hydrolysates can be addressed. This biopreservation approach holds promise for other meat products and contributes to the circular economy concept of the meat industry by valorizing slaughterhouse blood and producing new antilisterial compounds. Full article
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