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The Preparation, Purification, Characterization, and Evaluation of the Bioactivity of...
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The Preparation, Purification, Characterization, and Evaluation of the Bioactivity 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 (25 June 2023) | Viewed by 6560

Special Issue Editor

Dr. Aphichart Karnchanatat

E-Mail Website
Guest Editor
Center of Excellence in Bioconversion and Bioseparation for Platform Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, Thailand
Interests: bioactive peptide; protein chemistry; structure and function; enzyme biotechnology; natural products; nutraceutical; functional food

Special Issue Information

Dear Colleagues,

The supply of food, and especially proteins, is a global concern due to population growth and changes in social and demographic characteristics. Suppliers are pressured to deliver increasing quantities and different types of food to meet this growing demand. Proteins are essential dietary components, as macronutrients with a range of functions and structural properties. As well as providing nutrition, they control many vital bodily functions. The quality of a protein is closely linked to the amino acid content, in terms of essential amino acid ratios, the ease of undergoing hydrolysis when digestion occurs, and the effects of amino acid processing following digestion and absorption. Furthermore, the various different amino acid sequences which are encoded in the structure of the protein can also affect overall human health. There is a growing amount of attention focusing on bioactive peptides derived from foods, since these peptides have the potential to mitigate a number of harmful health conditions. The benefits of bioactive peptides are numerous, and include antioxidant, antidiabetic, antihypertensive, anti-inflammatory, anticancer, antimicrobial, and anti-aging properties. These qualities underline the importance of examining bioactive peptides in greater detail, considering their production, properties, bioaccessibility, potential for commercial applications, and their role in the field of structural bioinformatics. Novel findings concerning bioactive peptides may have significant implications for improving human health and may be commercially advantageous in the areas of nutraceuticals and functional food ingredients. In this Special Issue, the preparation of bioactive peptides will be examined, along with their isolation, structural elucidation, and functional characterization, as well as an assessment of their potential therapeutic applications, by investigating their effects when employed in cells or in animal models to treat various diseases. The development of bioactive peptides to play a role in the creation of novel drug candidates is also discussed. Review articles and reports of original research are warmly welcomed in this context.

Dr. Aphichart Karnchanatat
Guest Editor

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 proteins
  • bioactive peptides
  • antidiabetic
  • antihypertensive
  • anti-inflammatory
  • anticancer
  • antimicrobial
  • anti-aging
  • immunomodulatory activity
  • molecular docking
  • structure–activity relationship

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Published Papers (2 papers)

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Research

16 pages, 3562 KiB  
Article
The Anti-Inflammatory Mechanism of Flaxseed Linusorbs on Lipopolysaccharide-Induced RAW 264.7 Macrophages by Modulating TLR4/NF-κB/MAPK Pathway
by Jialong Li, Jing Chen, Ping Huang, Zizhe Cai, Ning Zhang, Yong Wang and Ying Li
Foods 2023, 12(12), 2398; https://doi.org/10.3390/foods12122398 - 16 Jun 2023
Cited by 11 | Viewed by 3212
Abstract
Flaxseed linusorbs (FLs), cyclic peptides derived from flaxseed oils, have shown multiple activities such as anticancer, antibacterial, and anti-inflammatory effects. However, the anti-inflammatory monomers of FLs and their mechanisms are still unclear. In this study, we have elucidated that FLs suppress the modulation [...] Read more.
Flaxseed linusorbs (FLs), cyclic peptides derived from flaxseed oils, have shown multiple activities such as anticancer, antibacterial, and anti-inflammatory effects. However, the anti-inflammatory monomers of FLs and their mechanisms are still unclear. In this study, we have elucidated that FLs suppress the modulation of NF-κB/MAPK signaling pathways by targeting the inhibition of activating TLR4 in LPS-induced RAW 264.7 cells. Therefore, the transcription and expression of inflammatory cytokines (i.e., TNF-α, IL-1β, and IL-6) and inflammatory mediator proteins (i.e., iNos and Cox-2) were significantly suppressed by FLs. In addition, an in silico study discovered that eight monomers of FLs showed high-affinity bindings with TLR4. In silico data combined with HPLC results indicated that FLA and FLE, accounting for 44%, were likely the major anti-inflammatory monomers in FLs. In summary, FLA and FLE were proposed as the main anti-inflammatory active cyclopeptides via hindering TLR4/NF-κB/MAPK signaling pathways, suggesting the potential use of food-derived FLs as natural anti-inflammatory supplements in a daily diet. Full article
(This article belongs to the Special Issue The Preparation, Purification, Characterization, and Evaluation of the Bioactivity of Bioactive Peptides Derived from Food)
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14 pages, 2261 KiB  
Article
Xanthine Oxidase Inhibitory Peptides from Larimichthys polyactis: Characterization and In Vitro/In Silico Evidence
by Xiaoling Chen, Weiliang Guan, Yujin Li, Jinjie Zhang and Luyun Cai
Foods 2023, 12(5), 982; https://doi.org/10.3390/foods12050982 - 25 Feb 2023
Cited by 19 | Viewed by 2742
Abstract
Hyperuricemia is linked to a variety of disorders that can have serious consequences for human health. Peptides that inhibit xanthine oxidase (XO) are expected to be a safe and effective functional ingredient for the treatment or relief of hyperuricemia. The goal of this [...] Read more.
Hyperuricemia is linked to a variety of disorders that can have serious consequences for human health. Peptides that inhibit xanthine oxidase (XO) are expected to be a safe and effective functional ingredient for the treatment or relief of hyperuricemia. The goal of this study was to discover whether papain small yellow croaker hydrolysates (SYCHs) have potent xanthine oxidase inhibitory (XOI) activity. The results showed that compared to the XOI activity of SYCHs (IC50 = 33.40 ± 0.26 mg/mL), peptides with a molecular weight (MW) of less than 3 kDa (UF-3) after ultrafiltration (UF) had stronger XOI activity, which was reduced to IC50 = 25.87 ± 0.16 mg/mL (p < 0.05). Two peptides were identified from UF-3 using nano-high-performance liquid chromatography–tandem mass spectrometry. These two peptides were chemically synthesized and tested for XOI activity in vitro. Trp-Asp-Asp-Met-Glu-Lys-Ile-Trp (WDDMEKIW) (p < 0.05) had the stronger XOI activity (IC50 = 3.16 ± 0.03 mM). The XOI activity IC50 of the other peptide, Ala-Pro-Pro-Glu-Arg-Lys-Tyr-Ser-Val-Trp (APPERKYSVW), was 5.86 ± 0.02 mM. According to amino acid sequence results, the peptides contained at least 50% hydrophobic amino acids, which might be responsible for reducing xanthine oxidase (XO) catalytic activity. Furthermore, the inhibition of the peptides (WDDMEKIW and APPERKYSVW) against XO may depend on their binding to the XO active site. According to molecular docking, certain peptides made from small yellow croaker proteins were able to bind to the XO active site through hydrogen bonds and hydrophobic interactions. The results of this work illuminate SYCHs as a promising functional candidate for the prevention of hyperuricemia. Full article
(This article belongs to the Special Issue The Preparation, Purification, Characterization, and Evaluation of the Bioactivity of Bioactive Peptides Derived from Food)
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