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Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus
- Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus
- La I.-J.; Eum D.-Y.; Gedi V.; Kim J.; Jeong B.; Yoon M.-Y.
- Ewha Authors
- 정병문; 김진흥
- SCOPUS Author ID
- 정병문; 김진흥
- Issue Date
- Journal Title
- Enzyme and Microbial Technology
- vol. 45, no. 4, pp. 261 - 266
- SCI; SCIE; SCOPUS
- Fructose-1,6-bisphosphate (FBP) aldolase, is a glycolytic enzyme that catalyzes the reversible condensation reaction of FBP to dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P). The aldolase gene from Aquifex aeolicus was subcloned, overexpressed in E. coli and purified to 95% homogeneity. The purified enzyme was activated by high concentrations of NH4+ and low concentrations of Co2+. The native molecular weight of the purified FBP aldolase was identified as 67 kDa (dimer) by gel filtration chromatography. The enzyme exhibits optimum pH at 6.5 and temperature at 90 °C. Based on the kinetic characterizations, the apparent Km was calculated to be 4.4 ± 0.07 mM, while Vmax was found to be 100 ± 0.02 μM min-1 mg protein-1. The recombinant protein showed extreme heat stability; no activity loss was observed even at 100 °C for 2 h. In addition, the thermophilic enzyme also showed higher stability against several organic solvents viz. acetonitrile, 1,4-dioxane, and methanol. With higher stability against both heat and organic solvents than any other class II aldolase, the A. aeolicus FBP aldolase is an attractive enzyme for use as a biocatalyst for industrial applications. © 2009 Elsevier Inc. All rights reserved.
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