Purification and Partial Characterization of Alkaline Xylanase from Escherichia coli Carrying pCX311
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
著者
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Kudo T
Inst. Physical And Chemical Res.(riken) Saitama Jpn
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HONDA Hiroshi
The Riken Institute
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KUDO Toshiaki
The Riken Institute
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HORIKOSHI Koki
The Riken Institute
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