Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific |
| |
Authors: | Suijie Wu Bin Liu Xiaobo Zhang |
| |
Institution: | (1) School of Life Sciences, Xiamen University, Xiamen 361005, People’s Republic of China;(2) Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, 178 Daxue Rd., Xiamen 361005, People’s Republic of China |
| |
Abstract: | A novel xylanase-producing thermophilic strain MT-1 was isolated from a deep-sea hydrothermal field in east Pacific. A xylanase gene encoding 331 amino-acid peptide from this isolate was cloned and expressed in Escherichia
coli. The recombinant xylanase exhibited maximum activity at 70°C and had an optimum pH of 7.0. It was active up to 90°C and showed activity over a wide pH ranging from 5.5 to 10.0. The crude xylanase presented similar properties in temperature and pH to those of the recombinant xylanase. The recombinant xylanase was stable in 1 mM of enzyme inhibitors (PMSF, EDTA, 2-ME or DTT) and in 0.1% detergents (Tween 20, Chaps or Triton X-100), whereas, it was strongly inhibited by sodium dodecyl sulfate (SDS) (1 mM). In addition, its catalytic function was stable in the presence of Li+, Na+ or K+. However, it was strongly inhibited by Ni2+, Mn2+, Co2+, Cu2+, Zn2+, Cd2+, Hg2+ and Al3+ (1 or 0.1 mM). The K
m and V
max of the recombinant xylanase for oat spelt xylan were calculated to be 1.579 mg/ml and 289 μmol/(min • mg), respectively. Our study, therefore, presented a rapid overexpression and purification of xylanase from deep-sea thermophile aimed at improving the enzyme yield for industrial applications and scientific research. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|