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Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application
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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: closed (10 May 2024) | Viewed by 22471

Special Issue Editors

Dr. Thao Le

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Guest Editor
Department of Food Science and Microbiology, Auckland University of Technology, Auckland, New Zealand
Interests: protein chemistry; proteomics; milk protein; plant protein
Prof. Dr. Hilton Deeth

E-Mail Website
Guest Editor
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

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Keywords

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

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Published Papers (9 papers)

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Research

18 pages, 1999 KiB  
Article
Effects of Laccase and Transglutaminase on the Physicochemical and Functional Properties of Hybrid Lupin and Whey Protein Powder
by Teguh Santoso, Thao M. Ho, Geerththana Vinothsankar, Kirsi Jouppila, Tony Chen, Adrian Owens, Masoumeh Pourseyed Lazarjani, Mustafa M. Farouk, Michelle L. Colgrave, Don Otter, Rothman Kam and Thao T. Le
Foods 2024, 13(13), 2090; https://doi.org/10.3390/foods13132090 - 1 Jul 2024
Viewed by 1365 | Correction
Abstract
Plant-based protein is considered a sustainable protein source and has increased in demand recently. However, products containing plant-based proteins require further modification to achieve the desired functionalities akin to those present in animal protein products. This study aimed to investigate the effects of [...] Read more.
Plant-based protein is considered a sustainable protein source and has increased in demand recently. However, products containing plant-based proteins require further modification to achieve the desired functionalities akin to those present in animal protein products. This study aimed to investigate the effects of enzymes as cross-linking reagents on the physicochemical and functional properties of hybrid plant- and animal-based proteins in which lupin and whey proteins were chosen as representatives, respectively. They were hybridised through enzymatic cross-linking using two laccases (laccase R, derived from Rhus vernicifera and laccase T, derived from Trametes versicolor) and transglutaminase (TG). The cross-linking experiments were conducted by mixing aqueous solutions of lupin flour and whey protein concentrate powder in a ratio of 1:1 of protein content under the conditions of pH 7, 40 °C for 20 h and in the presence of laccase T, laccase R, or TG. The cross-linked mixtures were freeze-dried, and the powders obtained were assessed for their cross-linking pattern, colour, charge distribution (ζ-potential), particle size, thermal stability, morphology, solubility, foaming and emulsifying properties, and total amino acid content. The findings showed that cross-linking with laccase R significantly improved the protein solubility, emulsion stability and foaming ability of the mixture, whereas these functionalities were lower in the TG-treated mixture due to extensive cross-linking. Furthermore, the mixture treated with laccase T turned brownish in colour and showed a decrease in total amino acid content which could be due to the enzyme’s oxidative cross-linking mechanism. Also, the occurrence of cross-linking in the lupin and whey mixture was indicated by changes in other investigated parameters such as particle size, ζ-potential, etc., as compared to the control samples. The obtained results suggested that enzymatic cross-linking, depending on the type of enzyme used, could impact the physicochemical and functional properties of hybrid plant- and animal-based proteins, potentially influencing their applications in food. Full article
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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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
by Yanee Srimarut, Apinya Phanphuet, Thanatorn Trithavisup, Wachiraya Rattanawongsa, Rattaporn Saenmuangchin, Annop Klamchuen and Yuwares Malila
Foods 2024, 13(1), 159; https://doi.org/10.3390/foods13010159 - 2 Jan 2024
Cited by 1 | Viewed by 2028
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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11 pages, 1332 KiB  
Article
Processing-Induced Markers in Proteins of Commercial Plant-Based Drinks in Relation to Compositional Aspects
by Ida Schwartz Roland, Miguel Aguilera-Toro, Søren Drud-Heydary Nielsen, Nina Aagaard Poulsen and Lotte Bach Larsen
Foods 2023, 12(17), 3282; https://doi.org/10.3390/foods12173282 - 1 Sep 2023
Cited by 2 | Viewed by 1428
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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16 pages, 4653 KiB  
Article
Development, Characterization and Resveratrol Delivery of Hollow Gliadin Nanoparticles: Advantages over Solid Gliadin Nanoparticles
by Duoduo Li, Zihao Wei and Xiaolong Li
Foods 2023, 12(13), 2436; https://doi.org/10.3390/foods12132436 - 21 Jun 2023
Cited by 6 | Viewed by 1718
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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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
by Elsa Mecha, Mara Lisa Alves, Andreia Bento da Silva, Ana Bárbara Pereira, Diego Rubiales, Maria Carlota Vaz Patto and Maria Rosário Bronze
Foods 2023, 12(7), 1383; https://doi.org/10.3390/foods12071383 - 24 Mar 2023
Cited by 3 | Viewed by 3265
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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Graphical abstract

18 pages, 10748 KiB  
Article
Structural and Thermal Characterization of Protein Isolates from Australian Lupin Varieties as Affected by Processing Conditions
by Lavaraj Devkota, Konstantina Kyriakopoulou, Robert Bergia and Sushil Dhital
Foods 2023, 12(5), 908; https://doi.org/10.3390/foods12050908 - 21 Feb 2023
Cited by 15 | Viewed by 2961
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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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
by Papungkorn Sangsawad, Sasikan Katemala, Danou Pao, Saranya Suwanangul, Rachasit Jeencham and Manote Sutheerawattananonda
Foods 2022, 11(23), 3931; https://doi.org/10.3390/foods11233931 - 5 Dec 2022
Cited by 7 | Viewed by 2399
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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13 pages, 1833 KiB  
Article
Preparation and Characterization of an Anticancer Peptide from Oriental Tonic Food Enteromorpha prolifera
by Xiaosi Lin, Le Dong, Qingdan Yan, Yibo Dong, Li Wang and Fang Wang
Foods 2022, 11(21), 3507; https://doi.org/10.3390/foods11213507 - 4 Nov 2022
Cited by 10 | Viewed by 2019
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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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
by Gbemisola J. Fadimu, Asgar Farahnaky, Harsharn Gill, Olusegun A. Olalere, Chee-Yuen Gan and Tuyen Truong
Foods 2022, 11(21), 3375; https://doi.org/10.3390/foods11213375 - 26 Oct 2022
Cited by 18 | Viewed by 3971
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
(This article belongs to the Special Issue Food Proteins and Bioactive Peptides: Novel Sources, Characteristic and Application)
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