Characterization of a Novel Alginate Lyase from Flavobacterium multivolum K-11
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概要
- 論文の詳細を見る
An alginate lyase was purified from an extracellular enzyme (commercial preparation) of Flavobacterium multivolum K-11 by successive column chromatographies, such as cation exchange, chromatofocusing, and gel filtration. The purified enzyme migrated as a single band on SDS-PAGE and analytical isoelectric focusing. The molecular weight of the enzyme was 32,000 by SDS-PAGE and 33,000 by HPLC gel filtration chromatography, and the pI of the enzyme was 8.2 on isoelectric focusing. The enzyme exhibited maximum activity at pH 7.5 and 40°C, and was stable between pH 6.0 and 9.0, and at temperatures up to 20°C. The enzyme activity was remarkably inhibited by chemical compounds such as SDS, MIA, TNBS, and N-bromosuccinimide, while EDTA and PCMB had no effect on the enzyme activity. The enzyme decomposed both the G-block (guluronic acid content; 89%) and the M-block (mannuronic content; 92%) at nearly equal rates, and produced several kinds of unsaturated oligomers. Because such activity of alginate lyase has not been reported, we believe that this is a novel alginate lyase.
- 社団法人 日本食品科学工学会の論文
著者
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Murakami K
Research And Development Department Kibun Food Chemifa Co. Ltd.
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Kusakabe Isao
Institute of Applied Biochemistry, University of Tsukuba
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YOSHIDA Shigeki
Institute of Applied Biochemistry, University of Tsukuba
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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
Institute of Applied Biochemistry, University of Tsukuba
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Takeuchi Toshio
Research And Development Department Kibun Food Chemifa Co. Ltd.
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Kusakabe Isao
Institute Of Applied Biochemistry University Of Tsukuba
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Yoshida Shigeki
Institute 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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