Purification and partial characterization of alkaline xylanase from Escherichia coli carrying pCX311.
Open Access
- 1 January 1985
- journal article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 49 (11) , 3165-3169
- https://doi.org/10.1271/bbb1961.49.3165
Abstract
Xylanase produced by E. coli HB101 carrying plasmid pCX311, which contains the xylanase A gene of alkalophilic Bacillus sp. strain C-125, was purified by ammonium sulfate precipitation, DEAE-cellulose column chromatography and Sephadex G-75 gel filtration. The purified enzyme had a molecular weight of 43, 000. The pH and temperature optima for its activity were 6-10 and 70°C, respectively. The enzyme retained full activity after incubation at 50°C for 10min. These enzymatic properties of the xylanase were almost the same as those of xylanase A. But this enzyme was less stable than xylanase A at low pHs. Furthermore, we could purify a larger amount of alkaline xylanase from E. coli than from alkalophilic Bacillus sp. strain C-125.Keywords
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