Purification and properties of an enzyme capable of degrading the polysaccharide of the cyanobacterium, Nostoc commune.
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.
Dasman
Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Kajiyama
Shin'ichiro
S
Okazawa
Atsushi
A
Fukusaki
Ei-ichiro
E
Kobayashi
Akio
A
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
D010446:Peptide Fragments; D011135:Polysaccharides, Bacterial; D006026:Glycoside Hydrolases