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

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 Nori...

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Published in:Chemical communications (Cambridge, England) England), 2011-01, Vol.47 (45), p.12307-12309
Main Authors: Jebors, Said, Tauran, Yannick, Aghajari, Nushin, Boudebbouze, Samira, Maguin, Emmanuelle, Haser, Richard, Coleman, Anthony W, Rhimi, Moez
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cited_by cdi_FETCH-LOGICAL-c352t-37a29f7e513388cb850895d0be85c725738132ebcb229eb35c00de18a24ab7613
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container_end_page 12309
container_issue 45
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container_title Chemical communications (Cambridge, England)
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creator Jebors, Said
Tauran, Yannick
Aghajari, Nushin
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description 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.
doi_str_mv 10.1039/c1cc14930j
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source Royal Society of Chemistry:Jisc Collections:Royal Society of Chemistry Read and Publish 2022-2024 (reading list)
subjects Aldose-Ketose Isomerases - metabolism
Hydrogen-Ion Concentration
Lactobacillus - enzymology
Lactobacillus sakei
Life Sciences
Magnesium - chemistry
Manganese - chemistry
Protein Stability
Temperature
title Supramolecular stabilization of acid tolerant L-arabinose isomerase from Lactobacillus sakei
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