Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules
The effect of a dielectric conical structure on the adsorption properties of an enzyme on mica was studied by atomic force microscopy (AFM) with the example of horseradish peroxidase (HRP). The cone used was a cellulose cone with a 60° apex angle. Namely, AFM allowed us to reveal an increase in the...
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2022-11-01
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| author | Yuri D. Ivanov Vadim Y. Tatur Ivan D. Shumov Andrey F. Kozlov Anastasia A. Valueva Irina A. Ivanova Maria O. Ershova Nina D. Ivanova Igor N. Stepanov Andrei A. Lukyanitsa Vadim S. Ziborov |
| author_facet | Yuri D. Ivanov Vadim Y. Tatur Ivan D. Shumov Andrey F. Kozlov Anastasia A. Valueva Irina A. Ivanova Maria O. Ershova Nina D. Ivanova Igor N. Stepanov Andrei A. Lukyanitsa Vadim S. Ziborov |
| author_sort | Yuri D. Ivanov |
| collection | DOAJ |
| description | The effect of a dielectric conical structure on the adsorption properties of an enzyme on mica was studied by atomic force microscopy (AFM) with the example of horseradish peroxidase (HRP). The cone used was a cellulose cone with a 60° apex angle. Namely, AFM allowed us to reveal an increase in the enzyme’s aggregation during its adsorption onto mica from the solution incubated near the cone apex for 40 min—as compared with the control enzyme samples incubated far away from the cone. In contrast, no change in the HRP adsorption properties was observed after shorter (10 min) incubation of the sample near the cone. The enzymatic activity of HRP was found to be the same for all the enzyme samples studied. Our findings should be considered upon designing biosensors (in particular, those intended for highly sensitive diagnostic applications) and bioreactors containing conical structural elements. Furthermore, since HRP is widely employed as a model enzyme in studies of external impacts on enzymes determining food quality, our data can be of use in the development of food-processing methods based on the use of electromagnetic radiation (microwave treatment, radiofrequency heating, etc.). |
| first_indexed | 2024-03-09T17:54:07Z |
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| institution | Directory Open Access Journal |
| issn | 2076-3417 |
| language | English |
| last_indexed | 2024-03-09T17:54:07Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
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| series | Applied Sciences |
| spelling | doaj.art-4cfb2caff5ab40d1a3f09665f2957ec02023-11-24T10:29:12ZengMDPI AGApplied Sciences2076-34172022-11-0112231199410.3390/app122311994Effect of a Conical Cellulose Structure on Horseradish Peroxidase BiomacromoleculesYuri D. Ivanov0Vadim Y. Tatur1Ivan D. Shumov2Andrey F. Kozlov3Anastasia A. Valueva4Irina A. Ivanova5Maria O. Ershova6Nina D. Ivanova7Igor N. Stepanov8Andrei A. Lukyanitsa9Vadim S. Ziborov10Institute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaFoundation of Perspective Technologies and Novations, Moscow 115682, RussiaInstitute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaInstitute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaInstitute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaInstitute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaInstitute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaFoundation of Perspective Technologies and Novations, Moscow 115682, RussiaFoundation of Perspective Technologies and Novations, Moscow 115682, RussiaFoundation of Perspective Technologies and Novations, Moscow 115682, RussiaInstitute of Biomedical Chemistry, Pogodinskaya Str., 10 Build. 8, Moscow 119121, RussiaThe effect of a dielectric conical structure on the adsorption properties of an enzyme on mica was studied by atomic force microscopy (AFM) with the example of horseradish peroxidase (HRP). The cone used was a cellulose cone with a 60° apex angle. Namely, AFM allowed us to reveal an increase in the enzyme’s aggregation during its adsorption onto mica from the solution incubated near the cone apex for 40 min—as compared with the control enzyme samples incubated far away from the cone. In contrast, no change in the HRP adsorption properties was observed after shorter (10 min) incubation of the sample near the cone. The enzymatic activity of HRP was found to be the same for all the enzyme samples studied. Our findings should be considered upon designing biosensors (in particular, those intended for highly sensitive diagnostic applications) and bioreactors containing conical structural elements. Furthermore, since HRP is widely employed as a model enzyme in studies of external impacts on enzymes determining food quality, our data can be of use in the development of food-processing methods based on the use of electromagnetic radiation (microwave treatment, radiofrequency heating, etc.).https://www.mdpi.com/2076-3417/12/23/11994atomic force microscopyhorseradish peroxidasecelluloseconical structureelectromagnetic fieldprotein aggregation |
| spellingShingle | Yuri D. Ivanov Vadim Y. Tatur Ivan D. Shumov Andrey F. Kozlov Anastasia A. Valueva Irina A. Ivanova Maria O. Ershova Nina D. Ivanova Igor N. Stepanov Andrei A. Lukyanitsa Vadim S. Ziborov Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules Applied Sciences atomic force microscopy horseradish peroxidase cellulose conical structure electromagnetic field protein aggregation |
| title | Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules |
| title_full | Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules |
| title_fullStr | Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules |
| title_full_unstemmed | Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules |
| title_short | Effect of a Conical Cellulose Structure on Horseradish Peroxidase Biomacromolecules |
| title_sort | effect of a conical cellulose structure on horseradish peroxidase biomacromolecules |
| topic | atomic force microscopy horseradish peroxidase cellulose conical structure electromagnetic field protein aggregation |
| url | https://www.mdpi.com/2076-3417/12/23/11994 |
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