title: Purification and characterization of microbial gellan lyase.
abstract: Gellan lyase was purified from the culture fluid of soil samples incubated in a medium containing gellan as a sole carbon source. The enzyme was a monomer with a molecular mass of 140 kDa and was most active at pH 7.5 and 45 degrees C. The enzyme was highly specific to gellan and lowered the viscosity of the polymer.
authors.affiliation: Central Research Institute, Maruha Co., Tsukuba City, Japan. hasimoto@food2.food.kyoto-u.ac.jp.
authors.forename: W
authors.initials: W
authors.lastname: Hashimoto
authors.forename: T
authors.initials: T
authors.lastname: Inose
authors.forename: H
authors.initials: H
authors.lastname: Nakajima
authors.forename: N
authors.initials: N
authors.lastname: Sato
authors.forename: S
authors.initials: S
authors.lastname: Kimura
authors.forename: K
authors.initials: K
authors.lastname: Murata
mesh_terms: D002240:Carbohydrate Sequence; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D011135:Polysaccharides, Bacterial / Q000737:chemistry; D012988:Soil Microbiology; D013379:Substrate Specificity; D014783:Viscosity
chemical_list: D011135:Polysaccharides, Bacterial; C048288:gellan gum; D011133:Polysaccharide-Lyases; C091406:gellan lyase