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Study of Bioactive Proteins and Peptides from Microbial and Food Origin

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Applied Chemistry".

Deadline for manuscript submissions: closed (31 March 2022) | Viewed by 4832

Special Issue Editors


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Guest Editor
Institute of Sciences of Food Production, Italian National Council of Research, ISPA-CNR, Bari, Italy
Interests: microbiology; antimicrobials; antibiotic resistance; natural compounds
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
Institute of Sciences of Food Production, Italian National Council of Research, ISPA-CNR, Bari, Italy
Interests: food proteins; bioactive peptides; natural antimicrobials; biofilms; bacterial physiology; proteomics
Special Issues, Collections and Topics in MDPI journals

E-Mail Website
Guest Editor
Department of Informatics, Modeling, Electronics and Systems Engineering (DIMES), University of Calabria, I-87036 Rende, Italy
Interests: transport phenomena; bioconversions; production of biofuels; extraction; membranes; biotechnology in the food industry; modeling; waste valorization
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Food-borne proteins and the related peptides are growing in interest due to their biological activity and their possibility of entering in either in preparations and supplements for food and pharmaceutical uses. Due the high costs in terms of water demand and carbon footprint, food proteins from food surplus or waste are increasingly addressing to fuel circular food chains, even supporting the value chain of novel foods. The same advantages concern the microbial and single cell proteins (SCP) proposed as advantageous alternative protein source recently leading to patented revolutionary foods. Based on the selected microorganisms and readily available substrates and waste streams, poorly studied peptides might also be secreted generating high-value products. Unfortunately, the health promoting properties of these products need an appropriate validation to support any nutritional and / or health claims before their commercial distribution. In addition to this, studies on this topic are still fragmented and suffer from the lack of efficient and sustainable enrichment- methodologies that also preserve their biological activity managing the safety risks. The main bottlenecks in these approaches are represented by the purification process of protein and peptides in order to match the yield maximization of target compounds, prevent deterioration and loss of functionality and finally accommodate the needs of industrial processing.

All the step over-mentioned should be finalised to their application in industrial process, following some requirements, like safety, resources optimization and sustainability. As consequence interest in bio process modeling and control is significantly increased in the research community, thanks also to new process approach. At the same time, consolidate technologies, like membrane separation processes and enzyme immobilization techniques could be continuously improved thanks to the research in new materials, new analytical method as well as new field of application. Sustainability, in terms of energy and environment represents another significant point of interest for the development for achievement of bioactive proteins and peptides

Accordingly, the aim of this Molecules Special Issue is to cover new findings on the sustainable production of proteins and peptides of food and pharmaceutical interest with special reference to efficient biotechnological strategies. Review articles that make substantial advances within this field will also be considered.

As Guest Editors of this Special Issue of Molecules, we therefore encourage scientists working in any field involving bioactive proteins and peptides from microbial and food sources addressed to industrial applications to contribute to recent research that may lead to significant advances in the area.

Dr. Leonardo Caputo
Dr. Laura Quintieri
Prof. Dr. Vincenza Calabrò
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. Molecules 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 2700 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

  • Protein foods
  • Biopeptides for food and pharmaceutical uses
  • Single cell proteins (SCP)
  • Peptidomic
  • Membrane processes
  • Industrial scale- up
  • Safety assessment
  • Sustainability
  • Bioreactors
  • Bioprocess modelling and control

Published Papers (2 papers)

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Research

14 pages, 1349 KiB  
Article
Foaming and Structural Studies on the Acidic Subunit of Amaranth 11S Globulin Modified with Antihypertensive Peptides as a Function of pH and Ionic Strength
by Dafnis Aguilar-Farrera, Jocksan I. Morales-Camacho, Edgar Espinosa-Hernández, Claudia G. Benítez-Cardoza, G. Janet Jara-Romero and Silvia Luna-Suárez
Molecules 2022, 27(11), 3538; https://doi.org/10.3390/molecules27113538 - 31 May 2022
Cited by 1 | Viewed by 1353
Abstract
Some studies aimed at revealing the relationship between protein structure and their functional properties. However, the majority of these reports have been carried out using protein isolates. There are limited reports on the possible relationship between the functional properties and the structure of [...] Read more.
Some studies aimed at revealing the relationship between protein structure and their functional properties. However, the majority of these reports have been carried out using protein isolates. There are limited reports on the possible relationship between the functional properties and the structure of a purified protein. In this work the amaranth 11S globulin acidic subunit (AAC) and five mutations of the same protein that were modified in their variable regions with antihypertensive peptides (VYVYVYVY and RIPP), were analyzed at two ionic strength (2.9 and 17.6 g/L NaCl) and pH (3.0–7.0). Results revealed better solubility for the proteins mutated at the terminal ends (AACM.1 and AACM.4) and lower solubility for the protein inserted with RIPP peptide. Spectroscopy studies revealed an increase of β-sheet structure at high salt concentration for all proteins. It was also observed that salt concentration acted as a modulator, which allowed a better foam features for all modified proteins limiting movement of side chains and reducing red-shifted displacement of λmax. All proteins showed foam capacity ranging from 76 to 93% although foam stability was twofold better for modified proteins than for AAC at high salt concentration. This study allowed better understanding about the structural changes that influence the foaming properties of engineered proteins. Full article
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15 pages, 1375 KiB  
Article
Donkey Milk Fermentation by Lactococcus lactis subsp. cremoris and Lactobacillus rhamnosus Affects the Antiviral and Antibacterial Milk Properties
by Simona Cirrincione, Anna Luganini, Cristina Lamberti, Marcello Manfredi, Laura Cavallarin, Maria Gabriella Giuffrida and Enrica Pessione
Molecules 2021, 26(16), 5100; https://doi.org/10.3390/molecules26165100 - 23 Aug 2021
Cited by 8 | Viewed by 2489
Abstract
Background: Milk is considered an important source of bioactive peptides, which can be produced by endogenous or starter bacteria, such as lactic acid bacteria, that are considered effective and safe producers of food-grade bioactive peptides. Among the various types of milk, donkey milk [...] Read more.
Background: Milk is considered an important source of bioactive peptides, which can be produced by endogenous or starter bacteria, such as lactic acid bacteria, that are considered effective and safe producers of food-grade bioactive peptides. Among the various types of milk, donkey milk has been gaining more and more attention for its nutraceutical properties. Methods: Lactobacillus rhamnosus 17D10 and Lactococcus lactis subsp. cremoris 40FEL3 were selected for their ability to produce peptides from donkey milk. The endogenous peptides and those obtained after bacterial fermentation were assayed for their antioxidant, antibacterial, and antiviral activities. The peptide mixtures were characterized by means of LC-MS/MS and then analyzed in silico using the Milk Bioactive Peptide DataBase. Results: The peptides produced by the two selected bacteria enhanced the antioxidant activity and reduced E. coli growth. Only the peptides produced by L. rhamnosus 17D10 were able to reduce S. aureus growth. All the peptide mixtures were able to inhibit the replication of HSV-1 by more than 50%. Seventeen peptides were found to have 60% sequence similarity with already known bioactive peptides. Conclusions: A lactic acid bacterium fermentation process is able to enhance the value of donkey milk through bioactivities that are important for human health. Full article
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