• DOI:10.1111/J.1365-2672.1990.TB01530.X
• Corpus ID: 85907980

Purification and properties of three types of xylanases produced by an alkalophilic actinomycete

@article{Tsujibo1990PurificationAP,
  title={Purification and properties of three types of xylanases produced by an alkalophilic actinomycete},
  author={Hiroshi Tsujibo and T Sakamoto and Norikazu Nishino and Tōru Hasegawa and Yoshihiko Inamori},
  journal={Journal of Applied Microbiology},
  year={1990},
  volume={69},
  pages={398-405}
}

• H. Tsujibo, T. Sakamoto, +2 authors Y. Inamori
• Published 1 September 1990
• Biology
• Journal of Applied Microbiology

Three types of xylanases (l,4-β-D-xylan xylanohydrolase, EC 3.2.1.8) were isolated from the culture filtrate of an alkalophilic actinornycete, Nocardiopsis dassonvillei subsp. alba OPC-18. The enzymes (X-I, X-II and X-III) were purified by acetone precipitation, chromatographies of DEAE-cellulofine A-800, Sephadex G-75 and preparative isoelectric focusing. The purified enzymes showed single bands on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The molecular weights of X-I, X-II and X-III were 23000, 23000 and 37000, respectively. The pIs were 4.9 (X-I), 5.3 (X-II) and 4.1 (X-III). The optimum pH levels for the activity of X-I and X-II were pH 7.0. X-III was also most active at pH 7.0, but 62.5% of the activity remained even at pH 11. The optimum temperatures for the activities of X-I and X-II were 60°C and that of X-III was 50°C. X-I and X-II were stable in the range of pH 6–10, and X-III was stable in the range of pH 8–12 until 40°C for 30 min.