Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 344562
Title Structural features of a hyperthermostable endo-beta-1,3-glucanase in solution and adsorbed on 'invisible' particles
Author(s) Koutsopoulos, S.; Oost, J. van der; Norde, W.
Source Biophysical Journal 88 (2005)1. - ISSN 0006-3495 - p. 467 - 474.
Department(s) Physical Chemistry and Colloid Science
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) archaeon pyrococcus-furiosus - time-resolved fluorescence - circular-dichroism - proteins - adsorption - peroxidase - interfaces - stability - mechanism
Abstract Conformational characteristics and the adsorption behavior of endo-ß-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. Adsorption offered further stabilization to the heat-stable enzyme and in the case of adsorption on Teflon its denaturation temperature was measured at 133°C, i.e., the highest experimentally determined for a protein. The maintenance of the active conformation and biological function particularly at high temperatures is important for applications in biocatalysis and biotechnology. With this study we also suggest that nature may employ adsorption as a complementary mode to maintain structural integrity of essential biomolecules at extreme conditions of temperature.
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