@article{oai:kanazawa-u.repo.nii.ac.jp:00010636,
 author = {Mohamed Morsy, Fatthy and Kuzuha, Satomi and Takani, Yayoi and Sakamoto, Toshio},
 issue = {5},
 journal = {The Journal of General and Applied Microbiology},
 month = {Jan},
 note = {The cyanobacterium Nostoc commune is adapted to the terrestrial environment and forms a visible colony in which the cells are embedded in extracellular polysaccharides (EPSs), which play a crucial role in the extreme desiccation tolerance of this organism. When natural colonies were immersed in water, degradation of the colonies occurred within 2 days and N. commune cells were released into the water. The activities that hydrolyze glycoside bonds in various N. commune fractions were examined using artificial nitrophenyl-linked sugars as substrates. A β-D-glucosidase purified from the water-soluble fraction was resistant to 20 min of boiling. The β-D-glucosidase, with a molecular mass of 20 kDa, was identified as a cyanobacterial fasciclin protein based on its N-terminal amino-acid sequence. The 36-kDa major protein in the water-soluble fraction was purified, and the N-terminal amino-acid sequence of the protein was found to be identical to that of the water-stress protein (WspA) of N. commune. This WspA protein also showed heat-resistant β-D-galactosidase activity. The fasciclin protein and WspA in the extracellular matrix may play a role in the hydrolysis of the EPSs surrounding the cells, possibly as an aid in the dispersal of cells, thus expanding the colonies of this cyanobacterium.},
 pages = {243--252},
 title = {Novel thermostable glycosidases in the extracellular matrix of the terrestrial cyanobacterium Nostoc commune},
 volume = {54},
 year = {2008}
}