Advances in Bioactive Proteins and Peptides from Plant Foods

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Physics and (Bio)Chemistry".

Deadline for manuscript submissions: closed (31 March 2024) | Viewed by 5623

Special Issue Editor

State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, China
Interests: plant-derived active protein; food-derived angiotensin converting enzyme (ACE) inhibitory peptides; antimicrobial peptides; antioxidant peptides; active peptide in plant-based yogurt; bioavailability

Special Issue Information

Dear Colleagues,

Many foods are rich in bioactive proteins and peptides with many beneficial health effects, which can be adapted to prepare nutraceuticals and functional foods for disease management while reducing the overreliance on drugs in combatting diseases. Plant-derived bioactive proteins and peptides have received a great amount of interest since they have antibacterial, antiviral, antifungal, anti-inflammatory, anticancer and other biological and physiological activities. For the wide application in functional foods and nutraceuticals, the research critically focuses on the extraction and purification of bioactive proteins/peptides from natural plant resources, protein hydrolysate, microbiological fermentation product; the relationship between structure and function of bioactive proteins and peptides; the role of bioactive peptides produced by plant-based fermented product; how to improve the bioavailability of bioactive proteins/peptides in vitro and in vivo. This will provide a deep understanding of how bioactive proteins and peptides from plant influence the nutrition and health properties of foods.

Dr. Xingfei Li
Guest Editor

Manuscript Submission Information

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Keywords

  • plant-derived bioactive protein/peptide
  • structure and function
  • bioavailability
  • extraction and purification
  • ACE inhibitory activity
  • antimicrobial activity
  • antioxidant activity
  • microbiological fermentation

Published Papers (4 papers)

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Research

20 pages, 2742 KiB  
Article
Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of Rumexpatientia L. ×Rumextianshanicus A. Los
by Chang Liu, Jianing Wang, Dan Hong, Zhou Chen, Siting Li, Aijin Ma and Yingmin Jia
Foods 2024, 13(7), 981; https://doi.org/10.3390/foods13070981 - 22 Mar 2024
Viewed by 1011
Abstract
Rumexpatientia L. ×Rumextianshanicus A. Los (RRL), known as “protein grass” in China, was recognized as a new food ingredient in 2021. However, the cultivation and product development of RRL are still at an early stage, and no peptide research has been reported. [...] Read more.
Rumexpatientia L. ×Rumextianshanicus A. Los (RRL), known as “protein grass” in China, was recognized as a new food ingredient in 2021. However, the cultivation and product development of RRL are still at an early stage, and no peptide research has been reported. In this study, two novel antioxidant peptides, LKPPF and LPFRP, were purified and identified from RRL and applied to H2O2-induced HepG2 cells to investigate their antioxidant properties. It was shown that 121 peptides were identified by ultrafiltration, gel filtration chromatography, and LC-MS/MS, while computer simulation and molecular docking indicated that LKPPF and LPFRP may have strong antioxidant properties. Both peptides were not cytotoxic to HepG2 cells at low concentrations and promoted cell growth, which effectively reduced the production of intracellular ROS and MDA, and increased cell viability and the enzymatic activities of SOD, GSH-Px, and CAT. Therefore, LKPPF and LPFRP, two peptides, possess strong antioxidant activity, which provides a theoretical basis for their potential as food additives or functional food supplements, but still need to be further investigated through animal models as well as cellular pathways. Full article
(This article belongs to the Special Issue Advances in Bioactive Proteins and Peptides from Plant Foods)
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20 pages, 1930 KiB  
Article
Fermentation Characteristics, Antinutritional Factor Level and Flavor Compounds of Soybean Whey Yogurt
by Xinyu Zhang, Jie Long, Jun Liu, Yufei Hua, Caimeng Zhang and Xingfei Li
Foods 2024, 13(2), 330; https://doi.org/10.3390/foods13020330 - 20 Jan 2024
Cited by 3 | Viewed by 1460
Abstract
Soybean whey contains high levels of off-flavors and anti-nutritional factors and is generally considered unsuitable for direct application in the food industry. In this work, to reduce beany off-flavors and anti-nutritional factors, and to improve its fermentation characteristics, soybean whey was treated with [...] Read more.
Soybean whey contains high levels of off-flavors and anti-nutritional factors and is generally considered unsuitable for direct application in the food industry. In this work, to reduce beany off-flavors and anti-nutritional factors, and to improve its fermentation characteristics, soybean whey was treated with electrodialysis desalination, vacuum concentration and lactic acid bacteria (LAB) fermentation. The results showed that electrodialysis desalination increased the fermentation rate and the number of viable lactic acid bacteria of soybean whey yogurt. More than 90% of the antinutritional factor level (urease and trypsin inhibitory activity) was removed due to high-temperature denaturation inactivation and LAB degradation. Concentrated desalted soybean whey yogurt (CDSWY) possessed larger values for firmness and consistency, and a denser network microstructure compared with undesalted yogurt. Over 90% of off-flavors including hexanal, 1-octen-3-ol and 1-octen-3-one were removed after electrodialysis desalination and concentration treatment. Meanwhile, the newly generated β-damascenone through carotenoid degradation and 2,3-butanedione improved the pleasant flavor and sensory quality of CDSWY, while the salty taste of CSWY lowered its sensory quality. This study provided a theoretical basis for better utilization of soybean whey to develop a plant-based yogurt like dairy yogurt. Full article
(This article belongs to the Special Issue Advances in Bioactive Proteins and Peptides from Plant Foods)
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18 pages, 11088 KiB  
Article
Development and Identification of Novel α-Glucosidase Inhibitory Peptides from Mulberry Leaves
by Fanghui Deng, Yihao Liang, Yuelei Lei, Shanbai Xiong, Jianhua Rong and Yang Hu
Foods 2023, 12(21), 3917; https://doi.org/10.3390/foods12213917 - 26 Oct 2023
Cited by 1 | Viewed by 1513
Abstract
The mulberry leaf is a botanical resource that possesses a substantial quantity of protein. In this study, alcalase hydrolysis conditions of mulberry leaf protein were optimized using the response surface method. The results showed that the optimum conditions were as follows: substrate protein [...] Read more.
The mulberry leaf is a botanical resource that possesses a substantial quantity of protein. In this study, alcalase hydrolysis conditions of mulberry leaf protein were optimized using the response surface method. The results showed that the optimum conditions were as follows: substrate protein concentration was 0.5% (w/v), enzymatic hydrolysis temperature was 53.0 °C, enzymatic hydrolysis time was 4.7 h, enzyme amount was 17,800 U/g, and pH was 10.5. Then mulberry leaf peptides were separated by ultrafiltration according to molecular weight. Peptides (<3 kDa) were screened and subsequently identified using LC-MS/MS after the evaluation of α-glucosidase inhibition across various fractions. Three novel potential bioactive peptides RWPFFAFM (1101.32 Da), AAGRLPGY (803.91 Da), and VVRDFHNA (957.04 Da) with the lowest average docking energy were screened for molecular dynamics simulation to examine their binding stability with enzymes in a 37 °C simulated human environment. Finally, they were prepared by solid phase synthesis for in vitro verification. The former two peptides exhibited better IC50 values (1.299 mM and 1.319 mM, respectively). These results suggest that the α-glucosidase inhibitory peptides from mulberry leaf protein are potential functional foods or drugs for diabetes treatment, but further in vivo studies are needed to identify the bioavailability and toxicity. Full article
(This article belongs to the Special Issue Advances in Bioactive Proteins and Peptides from Plant Foods)
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14 pages, 3783 KiB  
Article
Discovery of ACE Inhibitory Peptides Derived from Green Coffee Using In Silico and In Vitro Methods
by Haopeng Dai, Min He, Guilin Hu, Zhongrong Li, Abdulbaset Al-Romaima, Zhouwei Wu, Xiaocui Liu and Minghua Qiu
Foods 2023, 12(18), 3480; https://doi.org/10.3390/foods12183480 - 19 Sep 2023
Viewed by 1148
Abstract
Inhibition of angiotensin-I converting enzyme (ACE) is an important means of treating hypertension since it plays an important regulatory function in the renin-angiotensin system. The aim of this study was to investigate the ACE inhibitory effect of bioactive peptides from green coffee beans [...] Read more.
Inhibition of angiotensin-I converting enzyme (ACE) is an important means of treating hypertension since it plays an important regulatory function in the renin-angiotensin system. The aim of this study was to investigate the ACE inhibitory effect of bioactive peptides from green coffee beans using in silico and in vitro methods. Alcalase and thermolysin were employed to hydrolyze protein extract from coffee beans. Bioactive peptides were identified by LC-MS/MS analysis coupled with database searching. The potential bioactivities of peptides were predicted by in silico screening, among which five novel peptides may have ACE inhibitory activity. In vitro assay was carried out to determine the ACE inhibitory degree. Two peptides (IIPNEVY, ITPPVMLPP) were obtained with IC50 values of 57.54 and 40.37 μM, respectively. Furthermore, it was found that two inhibitors bound to the receptor protein on similar sites near the S1 active pocket of ACE to form stable enzyme–peptide complexes through molecular docking, and the Lineweaver–Burk plot showed that IIPNEVY was a noncompetitive inhibitor, and ITPPVMLPP was suggested to be a mixed-type inhibitor. Our study demonstrated that two peptides isolated from coffee have potential applications as antihypertensive agents. Full article
(This article belongs to the Special Issue Advances in Bioactive Proteins and Peptides from Plant Foods)
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