| Autor: |
SINMA, Kanokkorn, KHUCHAROENPHAISAN, Khwanchai, KITPREECHAVANICH, Vichien, TOKUYAMA, Shinji |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; October 2011, Vol. 75 Issue: 10 p1957-1963, 7p |
| Abstrakt: |
An extracellular thermostable xylanase produced by Saccharopolyspora pathumthaniensisS582 was purified 167-fold to homogeneity with a recovery yield of 12%. The purified xylanase appeared as a single protein band on SDS–PAGE, with a molecular mass of 36 kDa. The optimal temperature and pH of the xylanase were 70 °C and 6.5. The enzyme was stable within a pH range of 5.5–10.0. It retained its activity after incubation at 50 °C for 2 h. Its half lives at temperatures of 60 and 70 °C were 180 and 120 min respectively. Hydrolysis of beechwood xylan by the xylanase yielded xylobiose and xylose as major products. The enzyme acted specifically on xylan as an endo-type xylanase, and exhibited a Kmvalue of 3.92 mg/mL and a Vmaxvalue of 256 μmol/min/mg. Enzyme activity was completely inhibited by Hg2+, and was stimulated by Rb+and Cs+. The xylanase gene was cloned from genomic DNA of Saccharopolyspora pathumthaniensisS582 and sequenced. The ORF consisted of 1,107 bp and encoded 368 amino acid residues containing a putative signal peptide of 23 residues. This xylanase is a new member of family (GH) 10 that shows highest identity, of 63.4%, with a putative xylanase from Nocardiopsis dassonvilleisubsp. dassonvillei. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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