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Spectroscopy
Volume 24 (2010), Issue 3-4, Pages 349-353
http://dx.doi.org/10.3233/SPE-2010-0469

High stability of trehalose/maltose binding protein from Thermococcus litoralis makes it a good candidate as a sensitive element in biosensor systems for sugar control

Olga I. Povarova,1 Olga V. Stepanenko,1 Anna I. Sulatskaya,1 Irina M. Kuznetsova,1 Konstantin K. Turoverov,1 Maria Staiano,2 Annalisa Vitale,2 and Sabato D'Auria2

1Institute of Cytology of the Russian Academy of Sciences, Saint-Petersburg, Russia
2Institute of Protein Biochemistry CNR, Napoli, Italy

Copyright © 2010 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Fluorescence and circular dichroism in far-UV region were used to study the stability of trehalose/maltose binding protein (TMBP) from hyper thermophilic archaeon Thermococcus litoralis and its complex with glucose (TMBP/Glc). The evaluation of difference between free energy of native and unfolded state for TMBP and TMBP/Glc showed that both of them are several times higher than that of proteins from mesophilic organisms. Due to the high stability and innate ability to bind glucose this protein is a good candidate as a sensitive element in biosensor systems for sugar control.