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

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Title: Comparative study on general properties of alginate lyases from some marine gastropod mollusks
Authors: Hata, Mami Browse this author
Kumagai, Yuya Browse this author
Rahman, Mohammad Matiur Browse this author
Chiba, Satoru Browse this author
Tanaka, Hiroyuki Browse this author →KAKEN DB
Inoue, Akira Browse this author →KAKEN DB
Ojima, Takao Browse this author →KAKEN DB
Keywords: Alginate lyase
Gastropod
Mollusks
Polysaccharide-lyase family
Amino acid sequence
Issue Date: May-2009
Publisher: Springer Japan
Journal Title: Fisheries Science
Volume: 75
Issue: 3
Start Page: 755
End Page: 763
Publisher DOI: 10.1007/s12562-009-0079-z
Abstract: Alginate lyase (EC 4.2.2.3) 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 4.2.2.3) 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 www.springerlink.com
Type: article (author version)
URI: http://hdl.handle.net/2115/38478
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 尾島 孝男

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