African Journal of
Microbiology Research

  • Abbreviation: Afr. J. Microbiol. Res.
  • Language: English
  • ISSN: 1996-0808
  • DOI: 10.5897/AJMR
  • Start Year: 2007
  • Published Articles: 5232

Full Length Research Paper

Characterization of thermostable 2-deoxy-D-ribose-5-phosphate aldolase with broad temperature adaptability from Thermococcus onnurineus NA1

Xiao-pu Yin1, Qiu-yan Wang1, Shu-juan Zhao1, Peng-fei Du1, Kai-lin Xie1, Lihua Yang2, Peng Jin1, Jin-hua Liu2 and Tian Xie1*
1Center for Biomedicine and Health, Hangzhou Normal University, Hangzhou 310012, P. R. China. 2College of Material, Chemistry and Chemical Engineering, Hangzhou Normal University, Hangzhou 310012, P. R. China.
Email: [email protected]

  •  Accepted: 15 June 2011
  •  Published: 04 August 2011


The 2-deoxy-D-ribose-5-phosphate aldolase gene from Thermococcus onnurineus NA1was sub cloned, over expressed in Escherichia coli and purified to apparent homogeneity. Analysis of the sequence of gene revealed an n of 681 base pairs encoding 227 amino acids predicted to yield a protein having molecular mass 25.3 kDa. The enzyme activity was optimal at 60°C and showed broad temperature adaptability, retaining more than 30% of its maximum activity when assayed at 10 to 75°C. The recombinant protein was heat stable; no activity loss was observed even after incubation at 80°C for 10 min. In addition, the thermophilic enzyme showed a remarkable resistance to acetaldehyde; it retained more than 45% activity after exposure for 20 h to 250 mM acetaldehyde at 25°C.


Key words: 2-Deoxy-D-ribose-5-phosphate aldolase, thermostable enzyme, broad temperature adaptability.