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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 |
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container_end_page | 12309 |
container_issue | 45 |
container_start_page | 12307 |
container_title | Chemical communications (Cambridge, England) |
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creator | Jebors, Said Tauran, Yannick Aghajari, Nushin Boudebbouze, Samira Maguin, Emmanuelle Haser, Richard Coleman, Anthony W Rhimi, Moez |
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 |
format | article |
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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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