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

• Published in: Fisheries science 2009-05, Vol.75 (3), p.755-763
• Main Authors: Hata, M.(Hokkaido Univ., Hakodate (Japan)), Kumagai, Y, Rahman, M.M, Chiba, S, Tanaka, H, Inoue, A, Ojima, T
• Format: Article
• Language: English
• Subjects: Algae; ALGINATE; ALGINATES; ALGINATOS; Amino acids; Ammonium; Archeogastropoda; ARGININA; ARGININE; Bacteria; Biomedical and Life Sciences; Comparative analysis; Comparative studies; DIGESTION; ENZIMAS; ENZYME; ENZYMES; Fish & Wildlife Biology & Management; Food Science; Fractionation; Freshwater & Marine Ecology; GASTROPODA; HALIOTIDAE; Haliotis discus hannai; HEPATOPANCREAS; IMMUNOBLOTTING; Life Sciences; Littorina brevicula; Marine mollusks; Mesogastropoda; MOLLUSCA; Mollusks; Omphalius rusticus; Original Article; PHAEOPHYCEAE; Shellfish; Studies
• ISSN: 0919-9268; 1444-2906
• DOI: 10.1007/s12562-009-0079-z

Alginate lyase (EC 4.2.2.3) is an enzyme that splits glycosyl linkages of alginate chain via beta-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, 34, and 34 kDa were isolated from H. discus, H. iris, and O. rusticus, respectively. While three alginate lyases with molecular masses of 35, 32, 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.