Structural features of a hyperthermostable endo-beta-1,3-glucanase in solution and adsorbed on "invisible" particles.

ABSTRACT: Conformational characteristics and the adsorption behavior of endo-beta-1,3-glucanase from the hyperthermophilic microorganism Pyrococcus furiosus were studied by circular dichroism, steady-state and time-resolved fluorescence spectroscopy, and calorimetry in solution and in the adsorbed state. The adsorption isotherms were determined on two types of surfaces: hydrophobic Teflon and hydrophilic silica particles were specially designed so that they do not interact with light and therefore do not interfere with spectroscopic measurements. We present the most straightforward method to study structural features of adsorbed macromolecules in situ using common spectroscopic techniques. The enzyme was irreversibly adsorbed and immobilized in the adsorbed state even at high temperatures. Adsorptio

SUBMITTER: Koutsopoulos S 

PROVIDER: S-EPMC1305023 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature