Biochemical and thermodynamic characteristics of thermo-alkali-stable xylanase from a novel polyextr...
Biochemical and thermodynamic characteristics of thermo-alkali-stable xylanase from a novel polyextremophilic Bacillus halodurans TSEV1
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Tokyo: Springer Japan
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English
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Tokyo: Springer Japan
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Contents
The purified extracellular xylanase of polyextremophilic
Bacillus halodurans
TSEV1 has been visualized as a single band on SDS-PAGE and eluted as single peak by gel filtration, with a molecular mass of 40 kDa. The peptide finger print and cloned xylanase gene sequence analyses indicate that this enzyme belongs to GH family 10. The active site...
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Full title
Biochemical and thermodynamic characteristics of thermo-alkali-stable xylanase from a novel polyextremophilic Bacillus halodurans TSEV1
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TN_cdi_proquest_miscellaneous_1434028253
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1434028253
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ISSN
1431-0651
E-ISSN
1433-4909
DOI
10.1007/s00792-013-0565-1