View : 18 Download: 0

Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus

Title
Characterization of a extreme thermostable fructose-1,6-bisphosphate aldolase from hyperthermophilic bacterium Aquifex aeolicus
Authors
La I.-J.Eum D.-Y.Gedi V.Kim J.Jeong B.Yoon M.-Y.
Ewha Authors
정병문김진흥
SCOPUS Author ID
정병문scopus; 김진흥scopus
Issue Date
2009
Journal Title
Enzyme and Microbial Technology
ISSN
0141-0229JCR Link
Citation
vol. 45, no. 4, pp. 261 - 266
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
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.
DOI
10.1016/j.enzmictec.2009.06.012
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE