Experimental Evidence for the Role of Dynamics in pH-Dependent Enzymatic Activity.
J Phys Chem B
; 128(24): 5814-5822, 2024 Jun 20.
Article
em En
| MEDLINE
| ID: mdl-38726956
ABSTRACT
Enzymatic activity is heavily influenced by pH, but the rationale for the dynamical mechanism of pH-dependent enzymatic activity has not been fully understood. In this work, combined neutron scattering techniques, including quasielastic neutron scattering (QENS) and small angle neutron scattering (SANS), are used to study the structural and dynamic changes of a model enzyme, xylanase, under different pH and temperature environments. The QENS results reveal that xylanase at optimal pH exhibits faster relaxational dynamics and a lower energy barrier between conformational substates. The SANS results demonstrate that pH affects both xylanase's stability and monodispersity. Our findings indicate that enzymes have optimized stability and function under their optimal pH conditions, with both structure and dynamics being affected. The current study offers valuable insights into enzymatic functionality mechanisms, allowing for broad industrial applications.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Temperatura
/
Difração de Nêutrons
/
Endo-1,4-beta-Xilanases
/
Espalhamento a Baixo Ângulo
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
China