ISSN 2736-1756
Advanced Journal of Microbiology Research ISSN 2241-9837 Vol. 13 (3), pp. 001-007, March, 2019. © International Scholars Journals
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.
Accepted 15 January, 2019
Abstract
The 2-deoxy-D-ribose-5-phosphate aldolase gene from Thermococcus onnurineus NA1 was 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.