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Foods
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Bioactivity of Protein Hydrolysates Extracted from Foods
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Bioactivity of Protein Hydrolysates Extracted from Foods

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Nutraceuticals, Functional Foods, and Novel Foods".

Deadline for manuscript submissions: closed (1 August 2023) | Viewed by 6193

Special Issue Editor

Prof. Dr. Adam Wasko

E-Mail Website
Guest Editor
Department of Biotechnology, Microbiology and Human Nutrition, Faculty of Food Science and Biotechnology, University of Life Sciences in Lublin, Lublin, Poland
Interests: lactic acid bacteria; PCR; molecular biology; genetics; microbiology; food safety; food microbiology; antibacterial activity; probiotics; bacteriocins; bioactive peptides; foodborne pathogens; fermentation; functional foods
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein and bioactive peptides (BP), especially those derived from food, play important roles in the metabolic functions of living organisms and, consequently, in human health. Proteins from plant and animal origins are potential sources of a wide range of BPs encrypted in their structure. They can be classified based on their mode of action as antimicrobial, anti-thrombotic, antihypertensive, opioid, immunomodulatory, mineral binding, and antioxidative. Enzymatic hydrolysis is the most effective method of producing functional hydrolysates or bioactive peptides. Moreover, the correlation between structure and functional properties is still not well understood; therefore, crude extracts, known as hydrolysates, are often acceptable and used widely in practice. Although there have been many results and findings in the functionalities of bioactive hydrolysates or peptides originated from food proteins, there is still a hole between basic knowledge and practice. The objective of this Special Issue is therefore to highlight the existing knowledge of the various potential benefits of the bioactivity of protein hydrolisates in improving the nutritional and health-related properties of foods.

Prof. Dr. Adam Wasko
Guest Editor

Manuscript Submission Information

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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
  • enzymatic hydrolysis
  • putative bioactivity
  • protein hydrolisates
  • food proteins
  • phisiological activity
  • health benefit
  • bioinformatics predictions

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Published Papers (3 papers)

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Research

13 pages, 973 KiB  
Article
Egg Yolk as a New Source of Peptides with Antioxidant and Antimicrobial Properties
by Michał Czelej, Tomasz Czernecki, Katarzyna Garbacz, Jacek Wawrzykowski, Monika Jamioł, Katarzyna Michalak, Natalia Walczak, Agata Wilk and Adam Waśko
Foods 2023, 12(18), 3394; https://doi.org/10.3390/foods12183394 - 11 Sep 2023
Cited by 5 | Viewed by 2501
Abstract
A significant increase in interest in food-derived peptides obtained mostly through enzymatic reactions has been observed in the past few years. One of the best sources of bioactive peptides are defatted egg yolk proteins, which can potentially find application as high-quality nutritional supplements [...] Read more.
A significant increase in interest in food-derived peptides obtained mostly through enzymatic reactions has been observed in the past few years. One of the best sources of bioactive peptides are defatted egg yolk proteins, which can potentially find application as high-quality nutritional supplements for infants with cow’s milk protein intolerance and as natural preservatives. The aim of this study was to obtain peptides from defatted egg yolk protein, to study their antioxidant and antimicrobial properties, and to identify peptides with bioactive properties To control the course of the process, MALDI-TOF/MS (matrix-assisted laser desorption/ionization time-of flight/mass spectrometry) spectra were also examined. The peptide mixture obtained through enzyme digestion was tested for its antioxidant properties by measuring the scavenging activity in 2,2-diphenyl-1-picrylhydrazyl radical (DPPH•), 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) radical cation decolorization (ABTS•+), and ferric reducing activity (FRAP) assays. Antimicrobial activity was also studied. The peptide mixture exhibited significant antioxidant activity: DPPH—1776.66 ± 32.99, ABTS—390.43 ± 8.92, and FRAP—16.45 ± 0.19. The inhibition of bacterial growth by two concentrations of the peptide mixture was examined. The best result was obtained in Bacillus cereus, with an inhibition zone of 20.0 ± 1.0 and 10.7 ± 0.6 mm at the concentrations of 50 and 25 mg/mL, respectively. The results of the study suggest that the mixture of egg yolk peptides may exhibit a number of health-promoting properties. Full article
(This article belongs to the Special Issue Bioactivity of Protein Hydrolysates Extracted from Foods)
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11 pages, 2806 KiB  
Article
Activity Changes of the Peptic Lactoferrin Hydrolysate in Human Gastric Cancer AGS Cells in Response to Cu(II) or Mn(II) Addition
by Li-Ying Bo, Zhi-Qin Pan, Qiang Zhang, Chun-Li Song, Jian Ren and Xin-Huai Zhao
Foods 2023, 12(14), 2662; https://doi.org/10.3390/foods12142662 - 11 Jul 2023
Cited by 1 | Viewed by 1635
Abstract
Lactoferrin is an interesting bioactive protein in milk and can interact with various metal ions of trace elements such as copper, iron, manganese, and others. In this study, a lactoferrin hydrolysate (LFH) was generated from commercial bovine lactoferrin by protease pepsin, fortified with [...] Read more.
Lactoferrin is an interesting bioactive protein in milk and can interact with various metal ions of trace elements such as copper, iron, manganese, and others. In this study, a lactoferrin hydrolysate (LFH) was generated from commercial bovine lactoferrin by protease pepsin, fortified with Cu2+ (or Mn2+) at two levels of 0.64 and 1.28 (or 0.28 and 0.56) mg/g protein, respectively, and then measured for the resultant bioactivity changes in the well-differentiated human gastric cancer AGS cells. The assaying results indicated that the LFH and Cu/Mn-fortified products had long-term anti-proliferation on the cells, while the treated cells showed DNA fragmentation and increased apoptotic cell proportions. Regarding the control cells, the cells treated with the LFH and especially Cu/Mn-fortified LFH had remarkably up-regulated mRNA expression of caspase-3 and Bax by respective 1.21–3.23 and 2.23–2.83 folds, together with down-regulated mRNA expression Bcl-2 by 0.88–0.96 folds. Moreover, Western-blot assaying results also indicated that the cells exposed to the LFH and Cu/Mn-fortified LFH (especially Mn at higher level) for 24 h had an enhanced caspase-3 expression and increased ratio of Bax/Bcl-2. It can thus be concluded that the used Cu/Mn-addition to the LFH may lead to increased bioactivity in the AGS cells; to be more specific, the two metal ions at the used addition levels could endow LFH with a higher ability to cause cell apoptosis by activating caspase-3 and increasing the Bax/Bcl-2 ratio. Full article
(This article belongs to the Special Issue Bioactivity of Protein Hydrolysates Extracted from Foods)
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12 pages, 3123 KiB  
Article
Amino Acid Composition of a Chum Salmon (Oncorhynchus keta) Skin Gelatin Hydrolysate and Its Antiapoptotic Effects on Etoposide-Induced Osteoblasts
by Hong-Fang Liu, Xiao-Wen Pan, Hua-Qiang Li, Xiao-Nan Zhang and Xin-Huai Zhao
Foods 2023, 12(12), 2419; https://doi.org/10.3390/foods12122419 - 20 Jun 2023
Viewed by 1531
Abstract
A gelatin hydrolysate with a hydrolysis degree of 13.7% was generated using the skin gelatin of chum salmon (Oncorhynchus keta) and papain-catalyzed enzymatic hydrolysis. The results of analysis demonstrated that four amino acids, namely Ala, Gly, Pro, and 4-Hyp, were the [...] Read more.
A gelatin hydrolysate with a hydrolysis degree of 13.7% was generated using the skin gelatin of chum salmon (Oncorhynchus keta) and papain-catalyzed enzymatic hydrolysis. The results of analysis demonstrated that four amino acids, namely Ala, Gly, Pro, and 4-Hyp, were the most abundant in the obtained gelatin hydrolysate with measured molar percentages ranging from 7.2% to 35.4%; more importantly, the four amino acids accounted for 2/3 of the total measured amino acids. However, two amino acids, Cys and Tyr, were not detected in the generated gelatin hydrolysate. The experimental results indicated that the gelatin hydrolysate at a dose of 50 µg/mL could combat etoposide-induced apoptosis in human fetal osteoblasts (hFOB 1.19 cells), causing a decrease in the total apoptotic cells from 31.6% to 13.6% (via apoptotic prevention) or 13.3% to 11.8% (via apoptotic reversal). Meanwhile, the osteoblasts exposed to the gelatin hydrolysate showed expression changes for 157 genes (expression folds > 1.5-fold), among which JNKK, JNK1, and JNK3 were from the JNK family with a 1.5–2.7-fold downregulated expression. Furthermore, the protein expressions of JNKK, JNK1, JNK3, and Bax in the treated osteoblasts showed a 1.25–1.41 fold down-regulation, whereas JNK2 expression was not detected in the osteoblasts. It is thus suggested that gelatin hydrolysate is rich in the four amino acids and has an in vitro antiapoptotic effect on etoposide-stimulated osteoblasts via mitochondrial-mediated JNKK/JNK(1,3)/Bax downregulation. Full article
(This article belongs to the Special Issue Bioactivity of Protein Hydrolysates Extracted from Foods)
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