Special Issue "Bioactive Proteins and Peptides derived from Food"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioactives and Nutraceuticals".

Deadline for manuscript submissions: 30 June 2014

Special Issue Editor

Guest Editor
Prof. Dr. Eunice C.Y. Li-Chan
Food Nutrition and Health Program, The University of British Columbia, Vancouver, BC, V6T 1Z4, Canada
Website: http://www.landfood.ubc.ca/directory/faculty/professors-and-instructors/eunice-li-chan
E-Mail: eunice.li-chan@ubc.ca
Phone: +1 604 822 6182
Interests: functional foods and nutraceuticals; bioactive proteins and peptides from dairy and seafood; antihypertensive; hypoglycemic; antioxidants

Special Issue Information

Dear Colleagues,

The role of dietary factors in promoting health, beyond their contribution to meeting essential nutrient requirements, is well established from epidemiological evidence. In this regard, a plethora of studies has been conducted to elucidate the bioactive properties of food-derived phytochemicals or plant-based components. More recently, however, the spotlight has focused on the tremendous potential of bioactive proteins and peptides that are derived from food for application as functional foods and nutraceuticals to enhance health and reduce risk of disease.

This Special Issue aims to present current knowledge and research trends concerning bioactive food proteins, with particular emphasis on the bioactive hydrolysates and peptides derived from food proteins. Possible topics range from basic fundamental research on structure-function relationships and mechanisms of action, to applied research on issues relating to the production, isolation, and characterization of bioactive components, or to considerations regarding the stability, bioavailability, and sensory (or techno-functional) properties of such components when they are incorporated into functional foods.

Thank you for contributing to this timely and exciting Special Issue.

Prof. Dr. Eunice C. Y. Li-Chan
Guest Editor

Submission

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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed Open Access monthly 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 1600 CHF (Swiss Francs).


Keywords

  • bioactive food proteins
  • enzymatically-derived food protein hydrolysates
  • bioactive peptides derived from food proteins
  • mechanism of action for reducing risk of disease (e.g., cardiovascular disease, obesity, metabolic syndrome, diabetes, oxidative stress)
  • structure-function relationships; qsar; in silico analysis
  • production and characterization
  • functional (sensory, technological, stability, bioavailability) properties for incorporation as functional foods or nutraceuticals

Published Papers

No papers have been published in this special issue yet, see below for planned papers.

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Articlee
Title: Angiotensin I-converting Enzyme Inhibitory and Antioxidant Activity of Salmon (Salmo salar) Protein Hydrolysates Obtained via Hydrolysis.
Authors: Darewicz Małgorzata, Borawska Justyna, Minkiewicz Piotr and Iwaniak Anna
Affiliation: University of Warmia and Mazury in Olsztyn, Faculty of Food Science, Chair of Food Biochemistry, 10-719 Olsztyn-Kortowo, Poland
Abstract: The objective of the study was the molecular characterization of hydrolysates and peptides derived from salmon proteins. The biological activity of hydrolysates and peptides was determined during in silico and in vitro assays. The results obtained at various stages of hydrolysis supported the identification of antioxidant peptides and angiotensin-converting enzyme inhibitory peptides in amino acid sequences of salmon myofibrillar and sarcoplasmic proteins. Myofibrillar and sarcoplasmic proteins of the salmon are potential sources of antioxidant peptides and ACE inhibitory peptides. Antioxidant peptides and ACE inhibitory peptides are released during hydrolysis and simulated digestion of salmon proteins in the human digestive system.

Type of Paper: Article
Title: New peptides with potential antimicrobial activity derived from milk proteins - a bioinformatics study based on the BIOPEP database”
Author: Bartłomiej Dziuba and Marta Dziuba
Affiliation
: Chair of Industrial and Food Microbiology, University of Warmia and Mazury in Olsztyn, Faculty of Food Science, Olsztyn, Poland
Abstract: Search for new peptides with antimicrobial activity, encrypted in protein sequences, applying bioinformatics tools was conducted in the work. All 424 antimicrobial peptides, collected in BIOPEP database were characterized by following parameters: molecular weight, isoelectric point, number of amino acid residues, composition with share of acidic, basic, hydrophobic, polar, aliphatic amino acids, net charge at pH 7.0, aliphatic index, instability index, extinction coefficient, Boman index, half-life and GRAVY index. Results of this analysis showing structural similarity and arising from it the physico-chemical properties and the values of biological activity indicators were used to type peptides with potential antimicrobial activity, released /in silico/ from milk proteins by proteolytic enzymes. The most important in the process of selection was the charge at pH 7.0, presence of proline, lysine, cysteine residues and Boman index value of the peptide. Applying above criteria, eleven peptides with potential antimicrobial activity among all released during /in silico/ proteolysis of milk proteins was selected.

Type of Paper: Research
Title:
Peptides from amaranth and anti-atherosclerosis
Authors:
Alvaro Montoya-Rodríguez1,2 Elvira González de Mejía2, Cuauhtémoc Reyes-Moreno1, Jorge Milán-Carrillo1.
Affiliation:
1 Programa Regional del Noroeste para el Doctorado en Biotecnología, FCQB-UAS, Ciudad Universitaria, AP 1354, CP 80000, Culiacán, Sinaloa, México
2 Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, IL, 61801, United States
Abstract:
Amaranth (Amaranthus hypochondriacus) protein hydrolysates have shown potential anti-atherosclerotic effect by reducing the expression of proteins associated to LOX-1 signaling pathway. The objective of this study was to test pure peptides, originally present in amaranth protein hydrolysates, on markers associated with arteriosclerosis such as LOX-1, ICAM-1 and MMP-9 in THP-1 lipopolysaccharide-induced human like-macrophages. The expression of LOX-1 was reduced by HGSEPFGPR (50%) and RGDPFPWPWYSH (38%) at a concentration of 10 µM, relative to the control. Also HGSEPFGPR reduced the expression of ICAM-1 by 29%, while the expression of MMP-9 was reduced by 19% (HGSEPFGPR), 22% (RGDPFPWPWYSH) and 35% (RPRYPWRYT). In conclusion, amaranth peptides have an anti-atherosclerotic potential by reducing the expression of proteins associated with LOX-1 signaling pathway.
Key words:
Peptides, amaranth, atherosclerosis, LOX-1

Last update: 12 March 2014

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert