Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application

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

Deadline for manuscript submissions: 10 May 2024 | Viewed by 12755

Special Issue Editors

Department of Food Science and Microbiology, Auckland University of Technology, Auckland, New Zealand
Interests: protein chemistry; proteomics; milk protein; plant protein
School of Agriculture and Food Sciences, The University of Queensland, Brisbane, QLD 4072, Australia
Interests: dairy science and technology; UHT processing and products; whey proteins; thermal and nonthermal processing; new product development
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The world population is predicted to reach 9.7 billion people by 2050 with the expectation of a high demand in protein consumption. Protein is an important nutrient in the body’s growth and biological functions for which the bioactive peptides derived from the protein often possess higher bioactivity, e.g., antioxidant, antihypertensive, anti-cancer, anti-inflammatory, than the parent protein. Protein also plays a critical role in maintaining the functional properties of food products e.g., emulsifying, foaming, and water-binding. Traditionally, proteins originated from animal sources such as meat, poultry, fish, eggs and milk have been the main proteins in human diets. This trend has shifted towards plant-based proteins which have emerged as an acceptable alternative protein source for human consumption. Plant protein is viewed as a natural, eco-friendly, and sustainable food source, but can also contribute health benefits such as weight loss, satiety and lowered glycaemic index. For these reasons, there is renewed interest in plant protein as a food ingredient, complementing and, in some cases, replacing animal-based protein. However, plant proteins often lack one or more essential amino acids which the human body requires for protein biosynthesis. In addition, the poor functional properties of some plant proteins e.g., solubility and water-holding capacity, make them difficult to apply in many food applications regardless of their high fibre and antioxidant content. Animal-based protein on the other hand maintains a vital part in the food market due to its high essential amino acid content, biological value and functional properties, despite some adverse health claims e.g., risk of bowel cancer and dairy allergies. Adequate nutrition can be achieved with pure plant-based diets, however, with greater awareness in choosing plant types (e.g., combined cereal and pulses), especially for those who are allergic or sensitive to some plant proteins (e.g., vicilin and legumin in soybeans, peanuts, and tree nuts). This Special Issue is to highlight novel protein sources on the market as well as approaches to improve the properties and nutritional qualities such as digestibility and bioactivity of the present and new protein sources. Also, combining plant and animal proteins has potential to be a future protein consumption trend. In addition, challenges occurring in plant protein production and utilisation of plant protein in food applications are expected to be addressed in this Special Issue.

Dr. Thao Le
Prof. Dr. Hilton Deeth
Guest Editors

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

  • bioactive peptides
  • plant-based proteins
  • animal-based proteins
  • nutritional quality
  • functional properties

Published Papers (8 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

14 pages, 1846 KiB  
Article
Estimating In Vitro Protein Digestion and Protein Digestibility Corrected Amino Acid Score of Chicken Breasts Affected by White Striping and Wooden Breast Abnormalities
Foods 2024, 13(1), 159; https://doi.org/10.3390/foods13010159 - 02 Jan 2024
Viewed by 724
Abstract
An understanding regarding impacts of growth-related myopathies, i.e., white striping (WS) and wooden breast (WB), on the quality of dietary protein from cooked chicken breast is still limited. This study aimed at comparing protein content and in vitro protein digestion and estimating the [...] Read more.
An understanding regarding impacts of growth-related myopathies, i.e., white striping (WS) and wooden breast (WB), on the quality of dietary protein from cooked chicken breast is still limited. This study aimed at comparing protein content and in vitro protein digestion and estimating the in vitro protein digestibility corrected amino acid score (PDCAAS) of cooked chicken meat exhibiting different abnormality levels (i.e., normal, WS, and WS + WB). The results show that the WS + WB samples exhibited lower protein content, greater cooking loss, and greater lipid oxidation than those of normal samples (p < 0.05). No differences in protein carbonyls or the myofibril fragmentation index were found (p ≥ 0.05). Cooked samples were hydrolyzed in vitro using digestive enzyme mixtures that subsequently mimicked the enzymatic reactions in oral, gastric, and intestinal routes. The WS + WB samples exhibited greater values of free NH2 and degree of hydrolysis than the others at all digestion phases (p < 0.05), suggesting a greater proteolytic susceptibility. The in vitro PDCAAS of the WS + WB samples was greater than that of the other samples for pre-school children, school children, and adults (p < 0.05). Overall, the findings suggest that the cooked chicken breast with the WS + WB condition might provide greater protein digestibility and availability than WS and normal chicken breasts. Full article
Show Figures

Figure 1

11 pages, 1332 KiB  
Article
Processing-Induced Markers in Proteins of Commercial Plant-Based Drinks in Relation to Compositional Aspects
Foods 2023, 12(17), 3282; https://doi.org/10.3390/foods12173282 - 01 Sep 2023
Cited by 1 | Viewed by 788
Abstract
The consumption of plant-based drinks is increasing, but they represent a product category normally with lower protein content as compared with bovine milk. Furthermore, the products are highly processed and, therefore, the proteins in this product category may carry a significant processing history. [...] Read more.
The consumption of plant-based drinks is increasing, but they represent a product category normally with lower protein content as compared with bovine milk. Furthermore, the products are highly processed and, therefore, the proteins in this product category may carry a significant processing history. In the present study, a series of 17 freshly produced, commercially available plant-based drinks were benchmarked according to protein-quality parameters. The plant-based drinks represented different plant sources, as well as some mixed products, and were investigated relative to composition, aggregate sizes, presence of non-reducible proteins complexes, and level of processing-induced markers in the proteins. Processing-induced changes in the proteins were determined by a newly developed cocktail method, determining markers related to Maillard and dehydroalanine pathways, as well as intact lysine by triple quadrupole-multiple reaction monitoring-mass spectrometry. It was found that all drinks contained non-reducible protein complexes, but specifically, oat-based drinks represented the largest span contents of processing-induced markers within the proteins, which may relate to their inherent processing histories. Furthermore, it was shown that in products containing added sugar, Maillard reaction-related processing markers were increased over the dehydroalanine pathway. Full article
Show Figures

Figure 1

16 pages, 4653 KiB  
Article
Development, Characterization and Resveratrol Delivery of Hollow Gliadin Nanoparticles: Advantages over Solid Gliadin Nanoparticles
Foods 2023, 12(13), 2436; https://doi.org/10.3390/foods12132436 - 21 Jun 2023
Cited by 3 | Viewed by 937
Abstract
Hollow nanoparticles have attracted extensive attention due to their advantages such as high loading capacity and superior stability. However, the complexity of the preparation process and harmfulness of the used raw materials have limited their application in the food field. Based on this, [...] Read more.
Hollow nanoparticles have attracted extensive attention due to their advantages such as high loading capacity and superior stability. However, the complexity of the preparation process and harmfulness of the used raw materials have limited their application in the food field. Based on this, hollow gliadin nanoparticles (HGNPs) were developed using a Na2CO3 sacrificial template method. The findings of this study suggested that HGNPs could be regarded as a delivery system for resveratrol (Res) and they exhibited excellent delivery performance. Compared with solid gliadin nanoparticles (SGNPs), the HGNPs displayed smaller particle sizes, better physical stability, higher encapsulation efficiency, stronger resistance to ultraviolet light and a more sustained release of Res in the gastrointestinal tract. This work is of practical significance for the development and utilization of protein-based nanoparticles with hollow structures as a delivery system for sensitive bioactives. Full article
Show Figures

Graphical abstract

17 pages, 1997 KiB  
Article
High Inter- and Intra- Diversity of Amino Acid Content and Protein Digestibility Disclosed in Five Cool Season Legume Species with a Growing Market Demand
Foods 2023, 12(7), 1383; https://doi.org/10.3390/foods12071383 - 24 Mar 2023
Cited by 2 | Viewed by 2216
Abstract
Legumes have been sought as alternative protein sources to ensure food security and environmental sustainability. Characterizing their protein content and quality, including in underutilized grain legumes, e.g., grass pea, gives value to the legumes’ underexplored variability. To fill the gap of knowledge in [...] Read more.
Legumes have been sought as alternative protein sources to ensure food security and environmental sustainability. Characterizing their protein content and quality, including in underutilized grain legumes, e.g., grass pea, gives value to the legumes’ underexplored variability. To fill the gap of knowledge in legumes’ protein quality, for the first time, five extensive collections of cool season grain legumes were cropped under the same environmental conditions and further analyzed. Multivariate analysis showed the existent intra- and inter-species variability. The legume species with the highest protein content, grass pea, Lathyrus sativus (LS), was not the one with the overall highest individual amino acids content and in vitro protein digestibility. With these last characteristics lentil, Lens culinaris (LC), was highlighted. The highest average values of arginine (Arg), glutamic acid (Glu), and threonine (Thr) were found in LS and Vicia faba (VF). Cicer arietinum (CA) stood out as the species with the highest values of Thr and methionine (Met). Regarding the in vitro protein digestibility (IVPD), LC, followed by Pisum sativum (PS) and LS, were the legume species with the highest values. Ultimately, this study bought to the fore legume species that are not commonly used in western diets but have high adaptability to the European agricultural systems. Full article
Show Figures

Graphical abstract

18 pages, 10748 KiB  
Article
Structural and Thermal Characterization of Protein Isolates from Australian Lupin Varieties as Affected by Processing Conditions
Foods 2023, 12(5), 908; https://doi.org/10.3390/foods12050908 - 21 Feb 2023
Cited by 10 | Viewed by 2007
Abstract
Proteins from the full and defatted flours of L. angustifolius cv Jurien and L. albus cv Murringo were prepared using alkaline extraction and iso-electric precipitation. Isolates were either freeze dried or spray dried or pasteurized at 75 ± 3 °C/5 min before freeze-drying. [...] Read more.
Proteins from the full and defatted flours of L. angustifolius cv Jurien and L. albus cv Murringo were prepared using alkaline extraction and iso-electric precipitation. Isolates were either freeze dried or spray dried or pasteurized at 75 ± 3 °C/5 min before freeze-drying. Various structural properties were investigated to elucidate the varietal and processing-induced effect on molecular and secondary structure. Irrespective of processing, isolated proteins had a similar molecular size, with α-conglutin (412 kDa) and β-conglutin (210 kDa) being principal fractions for the albus and angustifolius variety, respectively. Smaller peptide fragments were observed for the pasteurized and spray dried samples, indicating some degree of processing-induced changes. Furthermore, secondary structure characterization by Fourier-transform-infrared and circular dichroism spectroscopy showed β-sheet and α-helical structure being the dominant structure, respectively. Thermal characterization showed two denaturation peaks corresponding to β-conglutin (Td = 85–89 °C) and α-conglutin (Td = 102–105 °C) fractions. However, the enthalpy values for α-conglutin denaturation were significantly higher for albus species, which corroborates well with higher amounts of heat stable α-conglutin present. Amino acid profile was similar for all samples with limiting sulphur amino acid. In summary, commercial processing conditions did not have a profound effect on the various structural properties of lupin protein isolates, and properties were mainly determined by varietal differences. Full article
Show Figures

Figure 1

13 pages, 3545 KiB  
Article
Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions
Foods 2022, 11(23), 3931; https://doi.org/10.3390/foods11233931 - 05 Dec 2022
Cited by 2 | Viewed by 1576
Abstract
Sericin, a byproduct of the silk industry, is an underutilized protein derived from the yellow silk cocoon. This research aimed to produce and characterize the bioactive peptides from sericin using various enzymatic hydrolysis methods. Alcalase, papain, neutrase, and protease were tested under their [...] Read more.
Sericin, a byproduct of the silk industry, is an underutilized protein derived from the yellow silk cocoon. This research aimed to produce and characterize the bioactive peptides from sericin using various enzymatic hydrolysis methods. Alcalase, papain, neutrase, and protease were tested under their respective digestion conditions. Among the enzymes tested, neutrase-catalyzed sericin into specific peptides with the strongest dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibitory properties. The peptides were subjected to a simulated in vitro gastrointestinal (GI) digestion in order to determine their stability. The GI peptides that were produced by neutrase hydrolysis continued to have the highest DPP-IV and ACE inhibitory activities. The neutrase -digested peptides were then fractionated via ultrafiltration; the peptide fraction with a molecular weight <3 kDa (UF3) inhibited DPP-IV and ACE activities. After being subjected to in vitro blood plasma hydrolysis, the UF3 was slightly degraded but retained its bioactivity. As a result of these findings, sericin peptides can be utilized as novel dietary ingredients that may alleviate some metabolic syndromes via the dual inhibitory properties of DPP-IV and ACE. Full article
Show Figures

Graphical abstract

13 pages, 1833 KiB  
Article
Preparation and Characterization of an Anticancer Peptide from Oriental Tonic Food Enteromorpha prolifera
Foods 2022, 11(21), 3507; https://doi.org/10.3390/foods11213507 - 04 Nov 2022
Cited by 3 | Viewed by 1420
Abstract
Enteromorpha prolifera (E. prolifera), a tonic food in East Asian countries, is frequently studied for their pharmaceutical and healthcare applications. However, limited research has focused on antitumor peptides derived from this edible seaweed. In this study, we aimed to investigate the [...] Read more.
Enteromorpha prolifera (E. prolifera), a tonic food in East Asian countries, is frequently studied for their pharmaceutical and healthcare applications. However, limited research has focused on antitumor peptides derived from this edible seaweed. In this study, we aimed to investigate the anticancer properties of peptides isolated from the hydrolysate of E. prolifera generated by a plethora of proteases including trypsin, papain, bromelain, and alkaline protease. The results showed that the hydrolysate produced by papain digestion exhibited remarkably stronger anticancer activity and was subjected to further purification by ultrafiltration and sequential chromatography. One heptapeptide, designated HTDT-6-2-3-2, showed significant antiproliferation activity towards several human cancer cell lines. The IC50 values for NCI-H460, HepG2, and A549 were 0.3686 ± 0.0935 mg/mL, 1.2564 ± 0.0548 mg/mL, and 0.9867 ± 0.0857 mg/mL, respectively. Moreover, results from flow cytometry confirmed that cell apoptosis was induced by HTDT-6-2-3-2 in a dose-dependent manner. The amino acid sequence for this heptapeptide, GPLGAGP, was characterized by Edman degradation and further verified by Liquid Chromatography-Tandem Mass Spectrometry. In silico analysis results suggested that XIAP could be a potential target for HTDT-6-2-3-2. Molecular docking simulation showed that HTDT-6-2-3-2 could occupy a shallow pocket in the BIR3 domain of XIAP, which is involved in the inhibitory effect of caspase-9 activation. In conclusion, this E. prolifera derived peptide exhibited strong anticancer properties, which could be explored for pharmaceutical applications. Full article
Show Figures

Graphical abstract

20 pages, 3192 KiB  
Article
In-Silico Analysis and Antidiabetic Effect of α-Amylase and α-Glucosidase Inhibitory Peptides from Lupin Protein Hydrolysate: Enzyme-Peptide Interaction Study Using Molecular Docking Approach
Foods 2022, 11(21), 3375; https://doi.org/10.3390/foods11213375 - 26 Oct 2022
Cited by 7 | Viewed by 2158
Abstract
The use of natural ingredients for managing diabetes is becoming more popular in recent times due to the several adverse effects associated with synthetic antidiabetic medications. In this study, we investigated the in vitro antidiabetic potential (through inhibition of α-glucosidase (AG) and α-amylase [...] Read more.
The use of natural ingredients for managing diabetes is becoming more popular in recent times due to the several adverse effects associated with synthetic antidiabetic medications. In this study, we investigated the in vitro antidiabetic potential (through inhibition of α-glucosidase (AG) and α-amylase (AA)) of hydrolysates from lupin proteins pretreated with ultrasound and hydrolyzed using alcalase (ACT) and flavourzyme (FCT). We further fractionated ACT and FCT into three molecular weight fractions. Unfractionated ACT and FCT showed significantly (p < 0.05) higher AG (IC50 value = 1.65 mg/mL and 1.91 mg/mL) and AA (IC50 value = 1.66 mg/mL and 1.98 mg/mL) inhibitory activities than their ultrafiltrated fractions, where lower IC50 values indicate higher inhibitory activities. Then, ACT and FCT were subjected to peptide sequencing using LC-MS-QTOF to identify the potential AG and AA inhibitors. Molecular docking was performed on peptides with the highest number of hotspots and PeptideRanker score to study their interactions with AG and AA enzymes. Among the peptides identified, SPRRF, FE, and RR were predicted to be the most active peptides against AG, while AA inhibitors were predicted to be RPR, PPGIP, and LRP. Overall, hydrolysates prepared from lupin proteins using alcalase and flavourzyme may be useful in formulating functional food for managing diabetics. Full article
Show Figures

Figure 1

Back to TopTop