Abstract:
:The gene coding for xylose isomerase from the thermophilic bacterium Fervidobacterium gondwanense was cloned and overexpressed in Escherichia coli. The produced xylose isomerase (XylA), which closely resembles counterparts from Thermotoga maritima and T. neapolitana, was purified and characterized. It is optimally active at 70 degrees C, pH 7.3, with a specific activity of 15.0 U/mg for the interconversion of glucose to fructose. When compared with T. maritima XylA at 85 degrees C, a higher catalytic efficiency was observed. Divalent metal ions Co2+ and Mg2+ were found to enhance the thermostability.
journal_name
Environ Technoljournal_title
Environmental technologyauthors
Kluskens LD,Zeilstra J,Geerling AC,de Vos WM,van der Oost Jdoi
10.1080/09593330903486673subject
Has Abstractpub_date
2010-09-01 00:00:00pages
1083-90issue
10eissn
0959-3330issn
1479-487Xjournal_volume
31pub_type
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