Issue |
E3S Web of Conf.
Volume 215, 2020
International Scientific Conference on Biotechnology and Food Technology (BFT-2020)
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Article Number | 01006 | |
Number of page(s) | 8 | |
Section | Modern Biotechnology in Food Safety and Quality | |
DOI | https://doi.org/10.1051/e3sconf/202021501006 | |
Published online | 02 December 2020 |
Study of hydrophobin-type proteins from Funalia trogii
St. Petersburg State Institute of Technology (Technical University), 190013, Moskovsky prospect, 26, St. Petersburg, Russia
* Corresponding author: xludin.ar@yandex.ru
Hydrophobins are low-molecular surface-active proteins of fungi with high surface activity and the ability to self-assemble at the interface. The unusual properties of hydrophobins open up possibilities for their application in various fields, including medicine and the food industry. The wide range of possible applications of hydrophobins makes it important to develop and improve technology for their isolation and purification. The aim of the study was to select methods for the extraction of hydrophobin-type proteins and to study the ability of the obtained extracts to modify the solid surface. The source of hydrophobins in this study was the biomass of the fungus Funalia trogii. Methods for the isolation of hydrophobin-type proteins were developed, including purification of the extract from ballast proteins, followed by the destruction of agglomerates of hydrophobin-type proteins using acids in high concentrations. The surface activity and the ability to modify the surface of the obtained proteins were evaluated. As a result, we obtained extracts containing hydrophobin-type proteins with high surface activity. Funalia trogii extracts are capable of changing the hydrophobicity of the surface and can be used in various industries.
© The Authors, published by EDP Sciences, 2020
This is an Open Access article distributed under the terms of the Creative Commons Attribution License 4.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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