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J Agric Food Chem. 2008 May 28;56(10):3623-7. doi: 10.1021/jf073511e. Epub 2008 Apr 30.

Dehydroascorbate reductase cDNA from sweet potato (Ipomoea batatas [L.] Lam): expression, enzyme properties, and kinetic studies.

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  • 1Institute of Bioscience and Biotechnology and Center for Marine Bioscience and Biotechnology, National Taiwan Ocean University, Keelung 202, Taiwan.

Abstract

A cDNA encoding a putative dehydroascorbate reductase (DHAR) was cloned from sweet potato. The deduced protein showed a high level of sequence homology with DHARs from other plants (67 to approximately 81%). Functional sweet potato DHAR was overexpressed and purified. The purified enzyme showed an active monomeric form on a 12% native PAGE. The protein's half-life of deactivation at 50 degrees C was 10.1 min, and its thermal inactivation rate constant K(d) was 6.4 x 10(-2) min(-1). The enzyme was stable in a broad pH range from 6.0-11.0 and in the presence of 0.8 M imidazole. The K(m) values for DHA and GSH were 0.19 and 2.38 mM, respectively.

PMID:
18444663
[PubMed - indexed for MEDLINE]
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