Pulsed electric fields act on tryptophan to inactivate α-amylase
| Autor: | Katsuyuki Takahashi, Takayuki Ohshima, T. Fujiwara, Masayoshi Matsui, Alexis Guionet, Koichi Takaki, Takanori Tanino, H. Sato |
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| Rok vydání: | 2021 |
| Předmět: |
010302 applied physics
chemistry.chemical_classification biology Organoleptic Food preservation Tryptophan Active site Protein aggregation Condensed Matter Physics 01 natural sciences 010305 fluids & plasmas Surfaces Coatings and Films Electronic Optical and Magnetic Materials Enzyme chemistry Electric field 0103 physical sciences biology.protein Biophysics Amylase Electrical and Electronic Engineering Biotechnology |
| Zdroj: | Journal of Electrostatics. 112:103597 |
| ISSN: | 0304-3886 |
| DOI: | 10.1016/j.elstat.2021.103597 |
| Popis: | Enzyme inactivation is a common industrial step of food preservation. Conventional method is based on heating, thus reduce organoleptic property and virtues of the products. We propose a non-thermal method of enzyme inactivation based on pulsed electric fields. By comparing the effect of electric fields, heating and oxidation on alpha-amylase, we have shown that the electric field targets the active site of the enzyme via the tryptophan, resulting in a conformational disruption. An electric pulse of 2.5–12.5 kV/cm, 10 μs and 0.02–0.6 J, repeated at 1–30 Hz for a total applied energy of 1440 J, partially denatured alpha-amylase, reducing activity by up to 70%; however, this was not followed by protein aggregation, as observed for heat treatment to 70 °C. Those results brought new understanding on the mechanism of pulsed electric fields action on proteins, and might lead in new application in food industry or in medicine. |
| Databáze: | OpenAIRE |
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