Optical resolution of racemic pantolactone with a novel fungal enzyme, lactonohydrolase
1995
Kataoka, M. | Shimizu, K. | Sakamoto, Kiyohiko | Yamada, Hitoshi | Shimizu, S.
A novel enzymatic process for the optical resolution of racemic pantolactone through the stereospecific hydrolysis of D-pantolactone by lactonohydrolase of Fusarium oxysporum is described. F. oxysporum cells were found to catalyze the stereoselective hydrolysis of the D-enantiomer of racemic pantolactone. With 135 g/1 DL-pantolactone as the substrate, 41% was hydrolyzed and pantoic acid with an optical purity of 90% enantiomeric excess (for D-pantoic acid) was formed.
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