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N-terminal fusion of a hyperthermophilic chitin-binding domain to xylose isomerase from Thermotoga neapolitana enhances kinetics and thermostability of both free and immobilized enzymes

Immobilization of a thermostable D-xylose isomerase (EC 5.3.1.5) from Thermotoga neapolitana 5068 (TNXI) on chitin beads was accomplished via a N-terminal fusion with a chitin-binding domain (CBD) from a hyperthermophilic chitinase produced by Pyrococcus furiosus (PF1233) to create a fusion protein...

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Bibliographic Details
Main Authors: Harris, James M., Epting, Kevin L., Kelly, Robert M.
Format: Artigo
Language:Inglês
Published: 2010
Subjects:
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3711014/
https://ncbi.nlm.nih.gov/pubmed/20730758
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/btpr.416
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