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Comparative study on general properties of alginate lyases from some marine gastropod mollusks

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タイトル: Comparative study on general properties of alginate lyases from some marine gastropod mollusks
著者: Hata, Mami 著作を一覧する
Kumagai, Yuya 著作を一覧する
Rahman, Mohammad Matiur 著作を一覧する
Chiba, Satoru 著作を一覧する
Tanaka, Hiroyuki 著作を一覧する
Inoue, Akira 著作を一覧する
Ojima, Takao 著作を一覧する
キーワード: Alginate lyase
Polysaccharide-lyase family
Amino acid sequence
発行日: 2009年 5月
出版者: Springer Japan
誌名: Fisheries Science
巻: 75
号: 3
開始ページ: 755
終了ページ: 763
出版社 DOI: 10.1007/s12562-009-0079-z
抄録: Alginate lyase (EC is an enzyme that splits glycosyl linkages of alginate chain via β-elimination producing unsaturated oligoalginates. This enzyme is widely distributed in herbivorous marine mollusks, brown algae, and marine and soil bacteria. In the present study, we determined the general properties and partial amino-acid sequences of alginate lyases from three Archeogastropoda, i.e., Haliotis discus hannai, H. iris, and Omphalius rusticus, and one Mesogastropoda, i.e., Littorina brevicula, in order to enrich the information about functional and structural diversity in gastropod alginate lyases. The alginate lyases were extracted from hepatopancreas of these animals and purified by ammonium sulfate fractionation followed by conventional column chromatography. Single alginate lyases with molecular masses of approximately 28 kDa, 34 kDa, and 34 kDa were isolated from H. discus, H. iris, and O. rusticus, respectively. While three alginate lyases with molecular masses of 35 kDa, 32 kDa, and 28 kDa were isolated from L. brevicula. These enzymes were identified as poly(M) lyase (EC since they preferably degraded poly(M)-rich substrate. Western blot analysis using an antiserum raised against H. discus enzyme suggested that H. iris, and O. rusticus enzymes shared similar primary/higher order structure with H. discus enzyme, but the L. brevicula enzymes did not. H. discus, H. iris, and O. rusticus enzymes were classified to polysaccharide-lyase family-14 by the analysis of partial amino-acid sequences, while the L. brevicula enzymes were not.
Rights: The original publication is available at
資料タイプ: article (author version)
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 尾島 孝男


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