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Bioactivity of Peptides and Proteins from Plant Derived Sources
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Bioactivity of Peptides and Proteins from Plant Derived Sources

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

Deadline for manuscript submissions: closed (31 January 2023) | Viewed by 5557

Special Issue Editor

Dr. Matthew Nosworthy

E-Mail Website
Guest Editor
Guelph Research & Development Centre, Agriculture and Agri-Food Canada, Guelph, ON N1G 5C9, Canada
Interests: peptides; legumes; proteins; bioactivity

Special Issue Information

Dear Colleagues,

Dietary protein has been a top trend among both consumers and product developers for almost a decade, with interest in plant-based protein sources rising significantly in recent years. While the nutritional aspects of a protein source are an essential attribute, there is a growing focus on whether certain proteins, or the small peptides produced subsequent to digestion, have additional health benefits. Given that that the bioactivity of plant-based proteins/peptides and their specific health outcomes is a wide research area, the theme of this Special Issue is broad. 

Studies that investigate the bioactivity of plant proteins/peptides in humans, animal models, or cell culture are welcome. Primary plant sources can include cereals, ancient grains, legumes, pulses, among others. Topics that can be considered include, but are not limited to, effects on satiety, muscle maintenance/growth, lipid metabolism, glucose metabolism, and cardiovascular disease. Studies based on understanding how different food preparation and processing methods alter protein/peptide bioactivity will also be considered.    

Dr. Matthew Nosworthy
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

  • plant protein
  • bioactive
  • peptide
  • legume
  • cereal
  • processing
  • diet
  • human health

Published Papers (3 papers)

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Research

14 pages, 3961 KiB  
Article
Identification of a Novel ACE Inhibitory Hexapeptide from Camellia Seed Cake and Evaluation of Its Stability
by Qiaonan Zhu, Jiawen Xue, Peng Wang, Xianbo Wang, Jiaojiao Zhang, Xuezhi Fang, Zhiping He and Fenghua Wu
Foods 2023, 12(3), 501; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12030501 - 21 Jan 2023
Cited by 6 | Viewed by 1510
Abstract
The camellia seed cake proteins (CP) used in this study were individually hydrolyzed with neutral protease, alkaline protease, papain, and trypsin. The results showed that the hydrolysate had the highest ACE inhibitory activity at 67.36 ± 0.80% after four hours of neutral protease [...] Read more.
The camellia seed cake proteins (CP) used in this study were individually hydrolyzed with neutral protease, alkaline protease, papain, and trypsin. The results showed that the hydrolysate had the highest ACE inhibitory activity at 67.36 ± 0.80% after four hours of neutral protease hydrolysis. Val-Val-Val-Pro-Gln-Asn (VVVPQN) was then obtained through ultrafiltration, Sephadex G-25 gel chromatography separation, LC-MS/MS analysis, and in silico screening. VVVPQN had ACE inhibitory activity with an IC50 value of 0.13 mg/mL (198.66 μmol/L), and it inhibited ACE in a non-competitive manner. The molecular docking indicated that VVVPQN can combine with ACE to form eight hydrogen bonds. The results of the stability study showed that VVVPQN maintained high ACE-inhibitory activity in weakly acidic and neutral environments and that heat treatment (20–80 °C) and Na+, Mg2+, as well as Fe3+ metal ions had little effect on the activity of VVVPQN. Moreover, it remained relatively stable after in vitro simulated gastrointestinal digestion. These results revealed that VVVPQN identified in camellia seed cake has the potential to be applied in functional food or antihypertensive drugs. Full article
(This article belongs to the Special Issue Bioactivity of Peptides and Proteins from Plant Derived Sources)
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19 pages, 3680 KiB  
Article
Optimization and Molecular Mechanism of Novel α-Glucosidase Inhibitory Peptides Derived from Camellia Seed Cake through Enzymatic Hydrolysis
by Yuanping Zhang, Fenghua Wu, Zhiping He, Xuezhi Fang and Xingquan Liu
Foods 2023, 12(2), 393; https://0-doi-org.brum.beds.ac.uk/10.3390/foods12020393 - 13 Jan 2023
Cited by 10 | Viewed by 1933
Abstract
In recent years, food-derived hypoglycemic peptides have received a lot of attention in the study of active peptides, but their anti-diabetic mechanism of action is not yet clear. In this study, camellia seed cake protein (CSCP) was used to prepare active peptides with [...] Read more.
In recent years, food-derived hypoglycemic peptides have received a lot of attention in the study of active peptides, but their anti-diabetic mechanism of action is not yet clear. In this study, camellia seed cake protein (CSCP) was used to prepare active peptides with α-glucosidase inhibition. The optimization of the preparation of camellia seed cake protein hydrolyzed peptides (CSCPH) was conducted via response surface methodology (RSM) using a protamex with α-glucosidase inhibition as an indicator. The optimal hydrolysis conditions were pH 7.11, 4300 U/g enzyme concentration, 50 °C hydrolysis temperature, and 3.95 h hydrolysis time. Under these conditions, the α-glucosidase inhibition rate of CSCPH was 58.70% (IC50 8.442 ± 0.33 mg/mL). The peptides with high α-glucosidase inhibitory activity were isolated from CSCPH by ultrafiltration and Sephadex G25. Leu-Leu-Val-Leu-Tyr-Tyr-Glu-Tyr (LLVLYYEY) and Leu-Leu-Leu-Leu-Pro-Ser-Tyr-Ser-Glu-Phe (LLLLPSYSEF) were identified and synthesized for the first time by Liquid chromatography electrospray ionisation tandem mass spectrometry (LC-ESI-MS/MS) analysis and virtual screening with IC50 values of 0.33 and 1.11 mM, respectively. Lineweaver-Burk analysis and molecular docking demonstrated that LLVLYYEY was a non-competitive inhibitor of α-glucosidase, whereas LLLLPSYSEF inhibited α-glucosidase, which displayed a mixed inhibition mechanism. The study suggests the possibility of using peptides from Camellia seed cake as hypoglycaemic compounds for the prevention and treatment of diabetes. Full article
(This article belongs to the Special Issue Bioactivity of Peptides and Proteins from Plant Derived Sources)
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13 pages, 3288 KiB  
Article
Soybean-Derived Tripeptide Leu–Ser–Trp (LSW) Protects Human Vascular Endothelial Cells from TNFα-Induced Oxidative Stress and Inflammation via Modulating TNFα Receptors and SIRT1
by Hongbing Fan, Khushwant S. Bhullar, Zihan Wang and Jianping Wu
Foods 2022, 11(21), 3372; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11213372 - 26 Oct 2022
Cited by 4 | Viewed by 1557
Abstract
Soybean is a rich source of high-quality proteins and an excellent food source of bioactive peptides. A tripeptide, Leu–Ser–Trp (LSW), was previously identified from soybean as an angiotensin-converting enzyme inhibitory peptide. In the present work, we further studied its antioxidant and anti-inflammatory activities [...] Read more.
Soybean is a rich source of high-quality proteins and an excellent food source of bioactive peptides. A tripeptide, Leu–Ser–Trp (LSW), was previously identified from soybean as an angiotensin-converting enzyme inhibitory peptide. In the present work, we further studied its antioxidant and anti-inflammatory activities in human vascular endothelial cells (EA.hy926) and elucidated the mechanisms underlying these biological activities. In tumor necrosis factor alpha (TNFα)-stimulated EA.hy926 cells, LSW significantly inhibited oxidative stress, both reduced superoxide and malondialdehyde levels (p < 0.001), owing to its free-radical-scavenging ability. LSW treatment also mitigated the elevated protein expression of vascular adhesion molecule-1 (p < 0.001) and cyclooxygenase 2 (p < 0.01) via inhibition of NF-κB and p38/JNK signaling, respectively. Additionally, LSW also inhibited the endogenous formation of TNFα and attenuated the expression of its two receptors in EA.hy926 cells. Furthermore, LSW upregulated sirtuin-1 level, which partially contributed to its anti-inflammatory activity. These results demonstrate the multiple roles of LSW in ameliorating vascular endothelial oxidative stress and inflammatory responses, which support its uses as a nutraceutical or functional food ingredient for combating endothelial dysfunction and cardiovascular diseases. Full article
(This article belongs to the Special Issue Bioactivity of Peptides and Proteins from Plant Derived Sources)
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