STABILITY OF SUGAR-BINDING PROTEINS: D-GALACTOSE/D-GLUCOSE-BINDING PROTEIN
FROM ESCHERICHIA COLI AND TREHALOSE/MALTOSE-BINDING PROTEIN
FROM THERMOCOCCUS LITORALIS
Olga V. Stepanenko,1 O. I. Povarova,1 A. V. Fonin,1, 2 Olesya V. Stepanenko 1
1 Institute of Cytology RAS, St. Petersburg,
and 2 St. Petersburg State Polytechnical University;
1 e-mail: sov@mail.cytspb.rssi.ru
In this work we studied the structure and stability of sugar-binding proteins from mesophilic and thermophilic
organisms which are of great importance for their possible use as sensing probe of biosensors aimed to
glucose detection in the blood. The data obtained revealed the stabilizing effect of ligands on the structures of
D-galactose/D-glucose-binding protein (GGBP) from Escherichia coli and trehalose/maltose-binding protein
from thermophilic bacterium Thermococcus litoralis. It was found that TMBP posses an increased stability as its
structure remains native even under heating up to 95 °C.
Key words: trehalose/maltose-binding protein, D-galactose/D-glucose-binding protein, protein stability, biosensor
| Pdf |
Back |
Contents |
Main |
