Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity
The disaccharide trehalose is accumulated in the cytoplasm of some organisms in response to harsh environmental conditions. Trehalose biosynthesis and accumulation are important for the survival of such organisms by protecting the structure and function of proteins and membranes. Trehalose affects t...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-06-01
|
| Series: | Catalysts |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4344/10/6/659 |
| _version_ | 1797565573235736576 |
|---|---|
| author | José G. Sampedro Miguel A. Rivera-Moran Salvador Uribe-Carvajal |
| author_facet | José G. Sampedro Miguel A. Rivera-Moran Salvador Uribe-Carvajal |
| author_sort | José G. Sampedro |
| collection | DOAJ |
| description | The disaccharide trehalose is accumulated in the cytoplasm of some organisms in response to harsh environmental conditions. Trehalose biosynthesis and accumulation are important for the survival of such organisms by protecting the structure and function of proteins and membranes. Trehalose affects the dynamics of proteins and water molecules in the bulk and the protein hydration shell. Enzyme catalysis and other processes dependent on protein dynamics are affected by the viscosity generated by trehalose, as described by the Kramers’ theory of rate reactions. Enzyme/protein stabilization by trehalose against thermal inactivation/unfolding is also explained by the viscosity mediated hindering of the thermally generated structural dynamics, as described by Kramers’ theory. The analysis of the relationship of viscosity–protein dynamics, and its effects on enzyme/protein function and other processes (thermal inactivation and unfolding/folding), is the focus of the present work regarding the disaccharide trehalose as the viscosity generating solute. Finally, trehalose is widely used (alone or in combination with other compounds) in the stabilization of enzymes in the laboratory and in biotechnological applications; hence, considering the effect of viscosity on catalysis and stability of enzymes may help to improve the results of trehalose in its diverse uses/applications. |
| first_indexed | 2024-03-10T19:14:03Z |
| format | Article |
| id | doaj.art-72f4a163158744828722c57fdf7f9a0b |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T19:14:03Z |
| publishDate | 2020-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-72f4a163158744828722c57fdf7f9a0b2023-11-20T03:33:33ZengMDPI AGCatalysts2073-43442020-06-0110665910.3390/catal10060659Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated ViscosityJosé G. Sampedro0Miguel A. Rivera-Moran1Salvador Uribe-Carvajal2Instituto de Física, Universidad Autónoma de San Luis Potosí, Manuel Nava 6, Zona Universitaria, San Luis Potosí C.P. 78290, MexicoInstituto de Física, Universidad Autónoma de San Luis Potosí, Manuel Nava 6, Zona Universitaria, San Luis Potosí C.P. 78290, MexicoInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de México C.P. 04510, MexicoThe disaccharide trehalose is accumulated in the cytoplasm of some organisms in response to harsh environmental conditions. Trehalose biosynthesis and accumulation are important for the survival of such organisms by protecting the structure and function of proteins and membranes. Trehalose affects the dynamics of proteins and water molecules in the bulk and the protein hydration shell. Enzyme catalysis and other processes dependent on protein dynamics are affected by the viscosity generated by trehalose, as described by the Kramers’ theory of rate reactions. Enzyme/protein stabilization by trehalose against thermal inactivation/unfolding is also explained by the viscosity mediated hindering of the thermally generated structural dynamics, as described by Kramers’ theory. The analysis of the relationship of viscosity–protein dynamics, and its effects on enzyme/protein function and other processes (thermal inactivation and unfolding/folding), is the focus of the present work regarding the disaccharide trehalose as the viscosity generating solute. Finally, trehalose is widely used (alone or in combination with other compounds) in the stabilization of enzymes in the laboratory and in biotechnological applications; hence, considering the effect of viscosity on catalysis and stability of enzymes may help to improve the results of trehalose in its diverse uses/applications.https://www.mdpi.com/2073-4344/10/6/659trehaloseviscosityenzymesprotein dynamicsKramers’ theoryprotein stabilization |
| spellingShingle | José G. Sampedro Miguel A. Rivera-Moran Salvador Uribe-Carvajal Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity Catalysts trehalose viscosity enzymes protein dynamics Kramers’ theory protein stabilization |
| title | Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity |
| title_full | Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity |
| title_fullStr | Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity |
| title_full_unstemmed | Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity |
| title_short | Kramers’ Theory and the Dependence of Enzyme Dynamics on Trehalose-Mediated Viscosity |
| title_sort | kramers theory and the dependence of enzyme dynamics on trehalose mediated viscosity |
| topic | trehalose viscosity enzymes protein dynamics Kramers’ theory protein stabilization |
| url | https://www.mdpi.com/2073-4344/10/6/659 |
| work_keys_str_mv | AT josegsampedro kramerstheoryandthedependenceofenzymedynamicsontrehalosemediatedviscosity AT miguelariveramoran kramerstheoryandthedependenceofenzymedynamicsontrehalosemediatedviscosity AT salvadoruribecarvajal kramerstheoryandthedependenceofenzymedynamicsontrehalosemediatedviscosity |