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Pulsed Power Applications for Protein Conformational Change and the Permeabilization of Agricultural Products

Authors :
Koichi Takaki
Katsuyuki Takahashi
Alexis Guionet
Takayuki Ohshima
Source :
Molecules, Vol 26, Iss 20, p 6288 (2021)
Publication Year :
2021
Publisher :
MDPI AG, 2021.

Abstract

Pulsed electric fields (PEFs), which are generated by pulsed power technologies, are being tested for their applicability in food processing through protein conformational change and the poration of cell membranes. In this article, enzyme activity change and the permeabilization of agricultural products using pulsed power technologies are reviewed as novel, nonthermal food processes. Compact pulsed power systems have been developed with repetitive operation and moderate output power for application in food processing. Firstly, the compact pulsed power systems for the enzyme activity change and permeabilization are outlined. Exposure to electric fields affects hydrogen bonds in the secondary and tertiary structures of proteins; as a result, the protein conformation is induced to be changed. The conformational change induces an activity change in enzymes such as α-amylase and peroxidase. Secondly, the conformational change in proteins and the induced protein functional change are reviewed. The permeabilization of agricultural products is caused through the poration of cell membranes by applying PEFs produced by pulsed discharges. The permeabilization of cell membranes can be used for the extraction of nutrients and health-promoting agents such as polyphenols and vitamins. The electrical poration can also be used as a pre-treatment for food drying and blanching processes. Finally, the permeabilization of cell membranes and its applications in food processing are reviewed.

Details

Language :
English
ISSN :
14203049
Volume :
26
Issue :
20
Database :
Directory of Open Access Journals
Journal :
Molecules
Publication Type :
Academic Journal
Accession number :
edsdoj.77327813d61b48ae8e63684dc30d6b48
Document Type :
article
Full Text :
https://doi.org/10.3390/molecules26206288