L-arabonate and D-galactonate production by expressing a versatile sugar dehydrogenase in metabolically engineered Escherichia coli.

Bioresour Technol

Energy and Environment Fusion Technology Center (E(2)FTC), Department of Energy and Biotechnology (DEB), Myongji University, Yongin-si, Gyeonggi-do 449-728, Republic of Korea. Electronic address:

Published: May 2014

AI Article Synopsis

  • The study showcases the use of a flexible enzyme, l-arabinose dehydrogenase (AraDH), from *Azospirillum brasilense* to produce L-arabonate and D-galactonate.
  • AraDH effectively works with both L-arabinose and D-galactose, utilizing different cofactors (NAD(+) and NADP(+)).
  • Engineered E. coli strains produced significant amounts of L-arabonate and D-galactonate, demonstrating AraDH's potential for industrial applications in sugar acid production.

Article Abstract

The production of L-arabonate and D-galactonate employing a versatile l-arabinose dehydrogenase (AraDH) from Azospirillum brasilense is presented. The promiscuity of AraDH is manifested by its appreciable activity towards L-arabinose and D-galactose as substrates, and NAD(+) and NADP(+) as cofactors. The AraDH was introduced into an engineered Escherichia coli with inactive L-arabinose or D-galactose metabolism, resulting in strains EMA2 and EWG4, respectively. EMA2 produced 43.9 g L(-1)L-arabonate with a productivity of 1.22 g L(-1)h(-1) and 99.1% (mol/mol) yield. After methanol precipitation, 92.6% of L-arabonate potassium salt was recovered with a purity of 88.8%. Meanwhile, EWG4 produced 24.0 g L(-1)D-galactonate, which is 36% higher than that of the strain carrying the specific d-galactose dehydrogenase. Overall results reveal that the versatility of AraDH to efficiently catalyze the formation of L-arabonate and D-galactonate could be a useful tool in advancing industrial viability for sugar acids production.

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Source
http://dx.doi.org/10.1016/j.biortech.2014.03.056DOI Listing

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