title: Purification and properties of an enzyme capable of degrading the polysaccharide of the cyanobacterium, Nostoc commune.
abstract: A novel Nostoc commune-polysaccharide (NPS)-degrading enzyme with a molecular mass of 128.5 kDa was purified from Paenibacillus glycanilyticus DS-1. The optimum pH and temperature of the enzyme activity were 5.5 and 35 degrees C, respectively. The enzyme completely degraded NPS to oligosaccharides, ranging from tetra to hexasaccharides and could degrade the xylan weakly whereas xanthan, gellan, cellulose, curdlan and p-nitrophenyl-beta-D-xylopyranoside were not degraded. Homology analysis of the N-terminal amino acid sequence of the NPS-degrading enzyme against the PIR and SWISS-PROT databases indicated that the sequence was not homologous to any other polysaccharide-degrading enzyme.
authors.affiliation: Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
authors.lastname: Dasman
authors.forename: Shin'ichiro
authors.initials: S
authors.lastname: Kajiyama
authors.forename: Atsushi
authors.initials: A
authors.lastname: Okazawa
authors.forename: Ei-ichiro
authors.initials: E
authors.lastname: Fukusaki
authors.forename: Akio
authors.initials: A
authors.lastname: Kobayashi
mesh_terms: D000595:Amino Acid Sequence; D001406:Bacillaceae / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D000458:Cyanobacteria / Q000737:chemistry*; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010446:Peptide Fragments / Q000737:chemistry; D011135:Polysaccharides, Bacterial / Q000737:chemistry*; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D010446:Peptide Fragments; D011135:Polysaccharides, Bacterial; D006026:Glycoside Hydrolases