Characterization of a recombinant thermostable D-lyxose isomerase from Dictyoglomus turgidum that produces D-lyxose from D-xylulose

Biotechnology Letters
Jin-Geun ChoiDeok-Kun Oh

Abstract

A putative D-lyxose isomerase from Dictyoglomus turgidum was purified with a specific activity of 19 U/mg for D-lyxose isomerization by heat treatment and affinity chromatography. The native enzyme was estimated as a 42 kDa dimer by gel-filtration chromatography. The activity of the enzyme was highest for D-lyxose, suggesting that it is a D-lyxose isomerase. The maximum activity of the enzyme was at pH 7.5 and 75°C in the presence of 0.5 mM Co(2+), with a half-life of 108 min, K(m) of 39 mM, and k(cat) of 3,570 1/min. The enzyme is the most thermostable D-lyxose isomerase among those characterized to date. It converted 500 g D-xylulose/l to 380 g D-lyxose/l after 2 h. This is the highest concentration and productivity of D-lyxose reported thus far.

References

Dec 26, 2006·Journal of Bacteriology·Eun-Ah ChoYu-Ryang Pyun
Jun 15, 2010·Journal of Bioscience and Bioengineering·Hyun-Jung KwonDeok-Kun Oh
Jul 10, 2010·Journal of Molecular Biology·Laura M van StaalduinenZongchao Jia
Jul 17, 2010·Applied Biochemistry and Biotechnology·Phillip BrummDavid Mead

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Citations

Jul 8, 2015·Applied Microbiology and Biotechnology·Wanmeng MuBo Jiang
Feb 3, 2018·Applied Microbiology and Biotechnology·Jiawei HuangWanmeng Mu
Jul 4, 2018·Applied Microbiology and Biotechnology·Zheng FangWanmeng Mu
Oct 23, 2019·Applied Microbiology and Biotechnology·Hao WuWanmeng Mu
Aug 24, 2021·Frontiers in Bioengineering and Biotechnology·Simone Antonio De RoseJennifer A Littlechild

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