Enzymatic Synthesis of Optically Pure (R)-(-)-Mandelic Acid and Other 2-Hydroxycarboxylic Acids: Screening for the Enzyme, and Its Purification, Characterization and Use

@inproceedings{Yamazaki1986EnzymaticSO,
  title={Enzymatic Synthesis of Optically Pure (R)-(-)-Mandelic Acid and Other 2-Hydroxycarboxylic Acids: Screening for the Enzyme, and Its Purification, Characterization and Use},
  author={Yoshimitsu Yamazaki and Hidekatsu Maeda},
  year={1986}
}
An enzyme that reduces benzoylformate with NADH to form (R)-mandelate was extracted from cells of Streptococcus faecalis IFO 12964 and purified to more than 95% purity as evidenced by gel electrophoresis. Physicochemical and enzymic properties were studied. From the substrate specificity, we concluded that the enzyme was a kind of (R)-2-hydroxyisocaproate dehydrogenase. Optically pure (R)-(—)-mandelic acid was prepared with the enzyme, NADH, and alcohol, formate or glucose dehydrogenase in 84… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 13 CITATIONS

Construction of an electro-enzymatic bioreactor for the production of (R)-mandelate from benzoylformate

VIEW 5 EXCERPTS
CITES METHODS & BACKGROUND
HIGHLY INFLUENCED

Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071.

VIEW 3 EXCERPTS
CITES BACKGROUND