Purification and Characterization of Extracellular Alginate Lyase from Enterobacter cloacae M-1
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概要
- 論文の詳細を見る
An alginate lyase from the culture supernatant of Enterobacter cloacae M-1 was purified by ammonium sulfate precipitation, cation-exchange chromatography (SP-Toyopearl), and gel filtration (Ultrogel AcA44). The final preparation thus obtained showed a single band on SDS-PAGE. The purified enzyme had the molecular weight of 38, 000 and 32, 000 by SDS-PAGE and gel filtration, respectively. The pI of the enzyme was 8. 9. The optimum pH and temperature for the enzyme reaction were around 7. 8 and 30℃, respectively. The enzyme was unstable on heating. EDTA completely inhibited the enzyme activity, but the activity was completely restored by the treatment with CaCl_2. The enzyme was specific for poly-guluronate and produced several kinds of unsaturated oligomers from the gluluronate. This suggested that the enzyme could be classified as an endo poly-guluronate lyase.
- 社団法人日本農芸化学会の論文
- 1995-04-23
著者
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Murakami K
Research And Development Department Kibun Food Chemifa Co. Ltd.
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MURATA Katsumi
Research Development Section, Kibun Food Chemifa Co., Ltd.
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TAKEUCHI Toshio
Research and Development Department, Kibun Food Chemifa Co., Ltd.
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Nibu Yutaka
lnstitute of Applied Biochemistry, University of Tsukuba
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Satoh Toshihide
lnstitute of Applied Biochemistry, University of Tsukuba
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Nishi Yuji
lnstitute of Applied Biochemistry, University of Tsukuba
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Kusakabe Isao
lnstitute of Applied Biochemistry, University of Tsukuba
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Murata K
Aoba Kasei Co. Ltd.
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Murata K
Kobe Oji Zoo Kobe Jpn
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Murata Kiyoshi
Aoba Kasei Co. Ltd.
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Takeuchi Toshio
Research And Development Department Kibun Food Chemifa Co. Ltd.
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Nishi Yuji
Lnstitute Of Applied Biochemistry University Of Tsukuba
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Kusakabe I
Univ. Tsukuba Tsukuba Jpn
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Nibu Yutaka
Lnstitute Of Applied Biochemistry University Of Tsukuba
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Satoh Toshihide
Lnstitute Of Applied Biochemistry University Of Tsukuba
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MURATA Katsumi
Research and Development Department, Kibun Food Chemifa Co., Ltd.
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