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Bioorg Med Chem Lett. 2014 Jan 1;24(1):173-6. doi: 10.1016/j.bmcl.2013.11.047. Epub 2013 Nov 27.

pH-rate profiles of L-arabinitol 4-dehydrogenase from Hypocrea jecorina and its application in L-xylulose production.

Author information

1
Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea; Institute of SK-KU Biomaterials, Konkuk University, Seoul 143-701, Republic of Korea; Department of Environmental Engineering, Konkuk University, Seoul 143-701, Republic of Korea.
2
Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea.
3
Department of Biomedical Sciences, University of Ulsan, College of Medicine, Seoul 138-736, Republic of Korea.
4
Institute of SK-KU Biomaterials, Konkuk University, Seoul 143-701, Republic of Korea; Department of Environmental Engineering, Konkuk University, Seoul 143-701, Republic of Korea. Electronic address: hankim@konkuk.ac.kr.
5
Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea; Institute of SK-KU Biomaterials, Konkuk University, Seoul 143-701, Republic of Korea. Electronic address: jkrhee@konkuk.ac.kr.

Abstract

l-Arabinitol 4-dehydrogenase (LAD) from Hypocrea jecorina (HjLAD) was cloned and overexpressed in Escherichia coli BL21 (DE3). The kinetics of l-arabinitol oxidation by NAD(+), catalyzed by HjLAD, was studied within the pH range of 7.0-9.5 at 25°C. The turnover number (kcat) and the catalytic efficiency (kcat/Km) were 4200min(-1) and 290mM(-1)min(-1), respectively. HjLAD showed the highest turnover number and catalytic efficiency among all previously characterized LADs. In further application of HjLAD, rare l-sugar l-xylulose was produced by the enzymatic oxidation of arabinitol to give a yield of approximately 86%.

KEYWORDS:

Molecular dynamics; Rare sugar; l-Xylulose; pH-Dependent kinetics

PMID:
24342239
DOI:
10.1016/j.bmcl.2013.11.047
[Indexed for MEDLINE]
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