title: Purification and determination of the action pattern of Haliotis tuberculata laminarinase.
abstract: The major laminarinase activity (EC 3.2.1.39) from the gastropodean marine mollusc Haliotis tuberculata was purified to homogeneity by cation exchange chromatography and its action pattern was investigated by HPAEC-PAD analysis of the degradation of various laminarin samples. It consists of a 60 kDa protein capable of depolymerizing the unbranched portions of the beta-(1-->3), beta-(1-->6)-glucan, down to laminaritriose. The enzyme operates via a molecular mechanism retaining the anomeric configuration. As the purified protein does not cleave the beta-(1-->6) linkages, it can be used for the structural analysis of laminarins.
authors.affiliation: Centre d'Etudes d'Océanographie et de Biologie Marine (CEOBM-CNRS UPR 9042) B.P. 74, Roscof, France.
authors.forename: V
authors.initials: V
authors.lastname: Lépagnol-Descamps
authors.forename: C
authors.initials: C
authors.lastname: Richard
authors.forename: M
authors.initials: M
authors.lastname: Lahaye
authors.forename: P
authors.initials: P
authors.lastname: Potin
authors.forename: J C
authors.initials: JC
authors.lastname: Yvin
authors.forename: B
authors.initials: B
authors.lastname: Kloareg
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002852:Chromatography, Ion Exchange; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000302:isolation & purification*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008974:Mollusca / Q000201:enzymology*; D011133:Polysaccharide-Lyases / Q000302:isolation & purification; D011487:Protein Conformation
chemical_list: D004693:Glucan Endo-1,3-beta-D-Glucosidase; D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase