Optical resolution of racemic pantolactone with a novel fungal enzyme,lactonohydrolase |
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| Authors: | M Kataoka K Shimizu K Sakamoto H Yamada S Shimizu |
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| Institution: | (1) Research Institute, Fuji Chemical Industries, 933 Takaoka, Toyama, Japan;(2) Present address: Faculty of Engineering, Toyama Prefectural University, Kosugi-machi, Imizu-gun, 939-03 Toyoma, Japan;(3) Present address: Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, 606-01 Sakyo-ku, Kyoto, Japan |
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| Abstract: | A novel enzymatic process for the optical resolution of racemic pantolactone through the stereo-specific 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/l 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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