Food Bioactive Peptides Improve Human Health

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

Deadline for manuscript submissions: closed (5 November 2023) | Viewed by 7019

Special Issue Editor


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Guest Editor
State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China
Interests: bioactive peptides; food proteins; enzymatic hydrolysis; functionality; protein structure; protein modification; protein-based delivery system; vegetable protein drinks

Special Issue Information

Dear Colleagues,

Bioactive peptides are specific protein fragments that have a positive impact on body functions and may ultimately influence health.

Food bioactive peptides, encrypted in food proteins, are latent until they are released from their parental protein. They are more bioavailable and less allergenic compared to their parental proteins, and are gaining increasing attention because of their health-promoting ability. Unlike synthetic pharmaceutical drugs, food bioactive peptides are more natural and have almost no side effects, thus qualifying them as an alternative to such drugs. In recent years, the demand for the application of food bioactive peptides in human nutrition and health has been increasing tremendously.

In this Special Issue of Foods, we are encouraging the submission of manuscripts focused on the study of health-improving attributes of food bioactive peptides such as antioxidative, mineral-binding, antihypertensive, immunomodulatory, antimicrobial, anti-allergenic, antithrombotic, anti-inflammatory, antidiabetic, hypocholesterolemic, and anticancer activities. We welcome papers related to the preparation, purification, characterization, and quantitative structure–activity relationship of food bioactive peptides. This Special Issue aims to gather the latest and novel advances and to be of interest to researchers and professionals in the field.

Prof. Dr. Xiangzhen Kong
Guest Editor

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Keywords

  • bioactive peptides
  • food proteins
  • enzymatic hydrolysis
  • bioactivity
  • health
  • nutrition
  • functional foods

Published Papers (4 papers)

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Research

14 pages, 2953 KiB  
Article
Identification and In Silico Simulation on Inhibitory Platelet-Activating Factor Acetyl Hydrolase Peptides from Dry-Cured Pork Coppa
by Mingming Li, Xin Zhang, Jiapeng Li, Linggao Liu, Qiujin Zhu, Chao Qu, Yunhan Zhang and Shouwei Wang
Foods 2023, 12(6), 1190; https://doi.org/10.3390/foods12061190 - 11 Mar 2023
Viewed by 1240
Abstract
The unique processing technology of dry-cured meat products leads to strong proteolysis, which produces numerous peptides. The purpose of this investigation was the systematic isolation, purification, and identification of potentially cardioprotective bioactive peptides from dry-cured pork coppa during processing. According to the results [...] Read more.
The unique processing technology of dry-cured meat products leads to strong proteolysis, which produces numerous peptides. The purpose of this investigation was the systematic isolation, purification, and identification of potentially cardioprotective bioactive peptides from dry-cured pork coppa during processing. According to the results of anti-platelet-activating factor acetyl hydrolase activity and radical scavenging ability in vitro, the inhibitory effect of M1F2 in purified fractions on cardiovascular inflammation was higher than that of M2F2. The peptide of M1F2 was identified by nano-liquid chromatography–tandem mass spectrometry. A total of 30 peptides were identified. Based on bioinformatics methods, including in silico analysis and molecular docking, LTDKPFL, VEAPPAKVP, KVPVPAPK, IPVPKK, and PIKRSP were identified as the most promising potential platelet-activating factor acetyl hydrolase inhibitory peptides. Overall, bioactive peptides produced during dry-cured pork coppa processing demonstrate positive effects on human health. Full article
(This article belongs to the Special Issue Food Bioactive Peptides Improve Human Health)
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15 pages, 3513 KiB  
Article
Identification and Molecular Binding Mechanism of Novel α-Glucosidase Inhibitory Peptides from Hot-Pressed Peanut Meal Protein Hydrolysates
by Xinyu Yang, Dan Wang, Yangyong Dai, Luping Zhao, Wentao Wang and Xiuzhen Ding
Foods 2023, 12(3), 663; https://doi.org/10.3390/foods12030663 - 3 Feb 2023
Cited by 9 | Viewed by 2070
Abstract
Hot-pressed peanut meal protein hydrolysates are rich in Arg residue, but there is a lack of research on their α-glucosidase inhibitory activity. In this study, different proteases were used to produce hot-pressed peanut meal protein hydrolysates (PMHs) to evaluate the α-glucosidase inhibitory activity. [...] Read more.
Hot-pressed peanut meal protein hydrolysates are rich in Arg residue, but there is a lack of research on their α-glucosidase inhibitory activity. In this study, different proteases were used to produce hot-pressed peanut meal protein hydrolysates (PMHs) to evaluate the α-glucosidase inhibitory activity. All PMHs showed good α-glucosidase inhibitory activity with the best inhibition effect coming from the dual enzyme system of Alcalase and Neutrase with an IC50 of 5.63 ± 0.19 mg/mL. The fractions with the highest inhibition effect were separated and purified using ultrafiltration and cation exchange chromatography. Four novel α-glucosidase inhibitory peptides (FYNPAAGR, PGVLPVAS, FFVPPSQQ, and FSYNPQAG) were identified by nano-HPLC-MS/MS and molecular docking. Molecular docking showed that peptides could occupy the active pocket of α-glucosidase through hydrogen bonding, hydrophobic interaction, salt bridges, and π-stacking, thus preventing the formation of complexes between α-glucosidase and the substrate. In addition, the α-glucosidase inhibitory activity of PMHs was stable against hot, pH treatment and in vitro gastrointestinal digestion. The study demonstrated that PMHs might be used as a natural anti-diabetic material with the potential to inhibit α-glucosidase. Full article
(This article belongs to the Special Issue Food Bioactive Peptides Improve Human Health)
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11 pages, 2136 KiB  
Article
Uptake of Flaxseed Dietary Linusorbs Modulates Regulatory Genes Including Induction of Heat Shock Proteins and Apoptosis
by Youn Young Shim, Timothy J. Tse, AkalRachna K. Saini, Young Jun Kim and Martin J. T. Reaney
Foods 2022, 11(23), 3761; https://doi.org/10.3390/foods11233761 - 22 Nov 2022
Cited by 3 | Viewed by 1260
Abstract
Flaxseed (Linum usitatissimum L.) is gaining popularity as a superfood due to its health-promoting properties. Mature flax grain includes an array of biologically active cyclic peptides or linusorbs (LOs, also known as cyclolinopeptides) that are synthesized from three or more ribosome-derived precursors. [...] Read more.
Flaxseed (Linum usitatissimum L.) is gaining popularity as a superfood due to its health-promoting properties. Mature flax grain includes an array of biologically active cyclic peptides or linusorbs (LOs, also known as cyclolinopeptides) that are synthesized from three or more ribosome-derived precursors. Two flaxseed orbitides, [1–9-NαC]-linusorb B3 and [1–9-NαC]-linusorb B2, suppress immunity, induce apoptosis in a cell line derived from human epithelial cancer cells (Calu-3), and inhibit T-cell proliferation, but the mechanism of LO action is unknown. LO-induced changes in gene expression in both nematode cultures and human cancer cell lines indicate that LOs promoted apoptosis. Specific evidence of LO bioactivity included: (1) distribution of LOs throughout the organism after flaxseed consumption; (2) induction of heat shock protein (HSP) 70A, an indicator of stress; (3) induction of apoptosis in Calu-3 cells; and (4) modulation of regulatory genes (determined by microarray analysis). In specific cancer cells, LOs induced apoptosis as well as HSPs in nematodes. The uptake of LOs from dietary sources indicates that these compounds might be suitable as delivery platforms for a variety of biologically active molecules for cancer therapy. Full article
(This article belongs to the Special Issue Food Bioactive Peptides Improve Human Health)
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25 pages, 5829 KiB  
Article
Antioxidant Activity, Functional Properties, and Cytoprotective Effects on HepG2 Cells of Tree Peony (Paeonia suffruticosa Andr.) Seed Protein Hydrolysate as Influenced by Molecular Weights Fractionation
by Yingying Wang, Yingqiu Li, Chenying Wang, Jinxing He and Haizhen Mo
Foods 2022, 11(17), 2592; https://doi.org/10.3390/foods11172592 - 26 Aug 2022
Cited by 9 | Viewed by 1743
Abstract
In recent years, plant protein hydrolysates have gained increased attention due to their superior antioxidant activity and potential to prevent several chronic diseases associated with oxidative stress. This study aimed to investigate the antioxidant activity, functional properties, and cytoprotective effects of the tree [...] Read more.
In recent years, plant protein hydrolysates have gained increased attention due to their superior antioxidant activity and potential to prevent several chronic diseases associated with oxidative stress. This study aimed to investigate the antioxidant activity, functional properties, and cytoprotective effects of the tree peony seed protein hydrolysate (TPSPH) with different molecular weights (MWs). The antioxidant activities were evaluated by DPPH, hydroxyl radicals scavenging, Fe2+ chelating, and inhibition of the β-carotene oxidation abilities. The protective effects and mechanism against oxidative stress were determined using H2O2-stressed HepG2 cells. MW > 30 kDa of TPSPH showed the highest radical scavenging (DPPH IC50 = 0.04, hydroxyl IC50 = 0.89 mg/mL) and inhibition of β-carotene oxidation (80.07% at 2.0 mg/mL) activity. Moreover, MW > 30 kDa possessed high hydrophobicity, emulsifying capacity, and abundant antioxidant amino acids (28.22% of hydrophobic amino acids and 8.3% of aromatic amino acids). MW 5–10 kDa exhibited more effective protection against H2O2-induced HepG2 cells, by reducing reactive oxygen species (ROS), malonaldehyde (MDA), lactate dehydrogenase (LDH), and activating antioxidant enzymes (superoxide dismutase and catalase). These results indicated the potential application of TPSPH as an antioxidant in food and functional foods. Full article
(This article belongs to the Special Issue Food Bioactive Peptides Improve Human Health)
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