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Food Biochemistry and Effects of Proteins and Peptides
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Food Biochemistry and Effects of Proteins and Peptides

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Food Science and Technology".

Deadline for manuscript submissions: closed (20 August 2023) | Viewed by 6760

Special Issue Editor

Prof. Dr. Piotr Minkiewicz

E-Mail Website
Guest Editor
Department of Food Biochemistry, Faculty of Food Science, University of Warmia and Mazury in Olsztyn, 10-726 Olsztyn, Kortowo, Poland
Interests: food proteins; mass spectrometry; chromatography; bioinformatics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Proteins and peptides are considered to be two of the most important food components. It is well-known that proteins are indispensable due to their nutritional value. The impact of proteins and peptides on the physicochemical and functional properties of food products belongs to the most important topics in food science. Proteins are the sources of bioactive peptides. On the other hand, some proteins derived from foods are allergens. New sources of proteins, as well as the modification of their properties during processing, may improve their physicochemical and functional properties and reduce allergenicity. An important area in food protein science is research concerning the discovery, purification and application of new enzymes (including proteinases). Denaturation, proteolysis and heat-induced chemical modifications of proteins are among contemporary topic areas of research. In turn, research on peptides is focused on discovery of their new bioactivities and new protein resources. Last but not least, the development of food science and technology requires progress in analytical methods.

This Special Issue, entitled “Role and Properties of Proteins and Peptides in Foods”, will cover a selection of recent research articles, short communications and reviews presenting research concerning proteins and peptides in food, including research and practical applications.

Prof. Dr. Piotr Minkiewicz
Guest Editor

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Keywords

  • physicochemical properties of food proteins and peptides
  • functional properties of food proteins and peptides
  • nutritional value of food proteins
  • bioactive, functional and taste-affecting peptides
  • allergenicity and its reduction
  • changes of proteins and peptides during processing
  • purification of enzymes and their role in technological processes
  • novel sources of proteins and peptides for application in foods
  • analysis of food proteins and peptides

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Published Papers (4 papers)

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Research

18 pages, 4110 KiB  
Article
In Silico Analysis of Individual Fractions of Bovine Casein as Precursors of Bioactive Peptides—Influence of Post-Translational Modifications
by Piotr Minkiewicz, Małgorzata Darewicz and Anna Iwaniak
Appl. Sci. 2023, 13(14), 8091; https://doi.org/10.3390/app13148091 - 11 Jul 2023
Cited by 2 | Viewed by 1269
Abstract
Bovine casein is one of the most known precursors of bioactive peptides among food proteins. Thus far, in silico investigations addressing casein have taken no account of the impact of modifications of amino acid residues on the feasibility of bioactive peptide release. The [...] Read more.
Bovine casein is one of the most known precursors of bioactive peptides among food proteins. Thus far, in silico investigations addressing casein have taken no account of the impact of modifications of amino acid residues on the feasibility of bioactive peptide release. The present study aimed to determine the effect of such modification on the possibility of release of bioactive peptides from casein during simulated digestion. The αs1-, αs2-, β-, and κ-casein sequences were deposited in the BIOPEP-UWM protein database considering phosphorylated amino acids, cysteine residues forming disulfide bridges, and pyroglutamic acid residues. The frequency of occurrence of bioactive fragments and the frequency of their release by digestive enzymes were determined for the analyzed modified and unmodified proteins. Peptides found exclusively in the sequences of unmodified proteins were deemed as false-positive results. From 1.74% (β-casein A2) to 4.41% (αs2-casein B and D) of the false-positive results were obtained for the total frequency of occurrence of bioactive fragments (sums of frequencies computed for all activities). In turn, from 1.78% (κ-casein B) to 9.18% (β-casein A2 and A3) of false-positive results were obtained for the predicted total frequency of release of bioactive peptides by the system of digestive enzymes (pepsin, trypsin, and chymotrypsin). Full article
(This article belongs to the Special Issue Food Biochemistry and Effects of Proteins and Peptides)
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15 pages, 2721 KiB  
Article
Peptide Mapping with LC-HRMS and In Silico Tools for Evaluation of Potential Allergenicity of Commercially Available Whey Protein Hydrolysates
by Anastassia Taivosalo, Irina Stulova, Mary-Liis Kütt, Tiina Kriščiunaite, Taivo Lints, Tatjana Gimaeva and Martti Tamm
Appl. Sci. 2023, 13(13), 7402; https://doi.org/10.3390/app13137402 - 22 Jun 2023
Cited by 1 | Viewed by 1464
Abstract
Hypoallergenic formulas containing hydrolyzed protein are intended for use by infants to prevent cow’s milk protein allergy. The degree of hydrolysis of epitopic areas determines the residual allergenicity of whey protein hydrolysates (WPHs). However, only amino-acid-based infant formulas (IFs) are considered entirely nonallergenic. [...] Read more.
Hypoallergenic formulas containing hydrolyzed protein are intended for use by infants to prevent cow’s milk protein allergy. The degree of hydrolysis of epitopic areas determines the residual allergenicity of whey protein hydrolysates (WPHs). However, only amino-acid-based infant formulas (IFs) are considered entirely nonallergenic. The aim of this study was to investigate four commercially available WPHs with different degree of hydrolysis (H1–H4) for potential allergenicity, by applying LC-HRMS analysis of peptides, and using in silico tools to search for the immunoglobulin (IgE)-binding allergenic epitopes from the Immune Epitope Database. Additionally, the molecular weight distribution of proteins and peptides in the WPHs was measured by SE-UPLC. Based on the peptide coverage and peptide-length distribution profiles, the WPHs showed different extents of hydrolysis: extensively (H1 and H2), partially (H3), and slightly hydrolyzed (H4). Altogether, numerous peptides related to 46 specific IgE-binding epitopes from β-lactoglobulin and α-lactalbumin were found in all the WPHs, regardless of their extent of hydrolysis. Sequence-based identification of the specific peptide composition, with an application of in silico tools, is a reliable approach for discovering the potential allergenicity of protein hydrolysates for IFs. Full article
(This article belongs to the Special Issue Food Biochemistry and Effects of Proteins and Peptides)
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10 pages, 2356 KiB  
Communication
Antioxidant and Hypoglycemic Activity of Sacha Inchi Meal Protein Hydrolysate
by Tianyu Shu, Kai Wang and Xuewu Zhang
Appl. Sci. 2023, 13(11), 6528; https://doi.org/10.3390/app13116528 - 27 May 2023
Cited by 1 | Viewed by 1451
Abstract
Sacha inchi meal (SIM) is the residue from the processing of the oil crop sacha inchi. In the present study, biological enzymolysis was performed on SIM protein to obtain hydrolysates, and then the antioxidant and hypoglycemic activities were evaluated. The results showed that [...] Read more.
Sacha inchi meal (SIM) is the residue from the processing of the oil crop sacha inchi. In the present study, biological enzymolysis was performed on SIM protein to obtain hydrolysates, and then the antioxidant and hypoglycemic activities were evaluated. The results showed that the scavenging rates of alkaline protease hydrolysate (SAl) and protamex hydrolysate (SPr) to ABTS free radicals were close to that of vitamin C at 5 mg/mL, amounting to 99.83 ± 0.33% and 100.00 ± 0.09%, respectively. The dipeptidyl peptidase (DPP-IV) inhibitory activities of SPr and SAl were also the highest, at the concentration of 2.5 mg/mL, their inhibition rates were 74.15 ± 0.68% and 56.38 ± 1.51%, respectively, with the IC50 values of 1.007 mg/mL and 2.130 mg/mL, respectively. Moreover, compared with the model group, all the hydrolysates increased the glucose consumption by 187.01–348.79% (at 800 μg/mL) in insulin-resistant HepG2 cells, which were better than positive drug Metformin. In conclusion, SIM protein hydrolysates have significant antioxidant and hypoglycemic activity in vitro; therefore, the hydrolysates could be used as for functional food and pharmaceutical development. Full article
(This article belongs to the Special Issue Food Biochemistry and Effects of Proteins and Peptides)
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19 pages, 4486 KiB  
Article
The Molecular Docking and Inhibition Kinetics of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Soft-Shelled Turtle Yolk
by Nhung Thi Phuong Nong, Christoper Caesar Yudho Sutopo, Wei-Ting Hung, Ping-Hsun Wu and Jue-Liang Hsu
Appl. Sci. 2022, 12(23), 12340; https://doi.org/10.3390/app122312340 - 2 Dec 2022
Cited by 4 | Viewed by 1929
Abstract
The soft-shelled turtle yolk (SSTY) protein hydrolysate contains a potential source of bioactive peptides. Our previous study found that five SSTY peptides (WLQL, LPSW, LPLF, VPGLAL and LVGLPL) showed moderate to high dipeptidyl peptidase IV (DPP-IV) inhibitory activities. This study further investigated their [...] Read more.
The soft-shelled turtle yolk (SSTY) protein hydrolysate contains a potential source of bioactive peptides. Our previous study found that five SSTY peptides (WLQL, LPSW, LPLF, VPGLAL and LVGLPL) showed moderate to high dipeptidyl peptidase IV (DPP-IV) inhibitory activities. This study further investigated their angiotensin-I-converting enzyme (ACE) inhibitory activity. Consequently, WLQL was identified as the most potent ACE inhibitory peptide with a remarkably low IC50 value (16.87 ± 0.54 µM). The Lineweaver–Burk plot analysis was performed for the characterization of the peptide’s inhibition mode and the inhibition kinetics was rationalized using the molecular docking simulation. The result revealed that WLQL would dock into the S1 pockets of ACE, while LPSW interacted with ACE’s secondary binding site. Further evaluation of the peptides’ stability against ACE involved a pre-incubation experiment. After 3 h of pre-incubation with ACE, the four peptides were hydrolyzed into smaller fragments with varying degrees, suggesting that they are substrate-type inhibitors. In contrast, LVGLPL can tolerate hydrolysis by ACE and act as a true inhibitor. Full article
(This article belongs to the Special Issue Food Biochemistry and Effects of Proteins and Peptides)
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