Issue 45, 2011
From the journal:

Chemical Communications

Supramolecular stabilization of acid tolerant l-arabinose isomerase from Lactobacillus sakei†

Said Jebors,a   Yannick Tauran,a   Nushin Aghajari,b   Samira Boudebbouze,c   Emmanuelle Maguin,c   Richard Haser,b   Anthony W. Coleman*a  and  Moez Rhimi*b  

* Corresponding authors

a LMI CNRS UMR 5615, Université de Lyon 1, Villeurbanne, France
E-mail: antony.coleman@adm.univ-lyon 1.fr
Tel: +33 4 4243 1027

b Laboratory for Biocrystallography and Structural Biology of Therapeutic Targets, “Bases Moléculaires et Structurales des Systèmes Infectieux” (BMSSI) UMR5086-CNRS/Université de Lyon 1, Institut de Biologie et Chimie des Protéines FR3302, 7 Passage du Vercors, F-69367 Lyon cedex 07, France
E-mail: m.rhimi@ibcp.fr, rhimimoez@yahoo.fr
Fax: +33 4 72 72 26 16
Tel: +33 4 72 72 26 34

c Institut National de la Recherche Agronomique, UMR 1319 Micalis, F-78350 Jouy-en-Josas, France

Abstract

L-Arabinose isomerase stability is a crucial criterion for the industrial application of this biocatalyst. Noria and NoriaPG are capable of increasing the L-arabinose isomerase stability not only at high temperatures but also at low pH. Such results highlight, for the first time, the use of the Noria series of molecules for protein stabilization and activation.

Graphical abstract: Supramolecular stabilization of acid tolerant l-arabinose isomerase from Lactobacillus sakei

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Article information

DOI
https://doi.org/10.1039/C1CC14930J
Article type
Communication
Submitted
09 Aug 2011
Accepted
11 Oct 2011
First published
20 Oct 2011

Chem. Commun., 2011,47, 12307-12309

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Supramolecular stabilization of acid tolerant L-arabinose isomerase from Lactobacillus sakei

S. Jebors, Y. Tauran, N. Aghajari, S. Boudebbouze, E. Maguin, R. Haser, A. W. Coleman and M. Rhimi, Chem. Commun., 2011, 47, 12307 DOI: 10.1039/C1CC14930J

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