Molecular cloning and biochemical characterization of a novel erythrose reductase from Candida magnoliae JH110.

ABSTRACT:

Background

Erythrose reductase (ER) catalyzes the final step of erythritol production, which is reducing erythrose to erythritol using NAD(P)H as a cofactor. ER has gained interest because of its importance in the production of erythritol, which has extremely low digestibility and approved safety for diabetics. Although ERs were purified and characterized from microbial sources, the entire primary structure and the corresponding DNA for ER still remain unknown in most of erythritol-producing yeasts. Candida magnoliae JH110 isolated from honeycombs produces a significant amount of erythritol, suggesting the presence of erythrose metabolizing enzymes. Here we provide the genetic sequence and functional characteristics of a novel NADPH-dependent ER from C. magnoliae JH110.

Results<

SUBMITTER: Lee DH 

PROVIDER: S-EPMC2902421 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature