OPTICAL RESOLUTION OF RACEMIC PANTOLACTONE WITH A NOVEL FUNGAL ENZYME, LACTONOHYDROLASE
OPTICAL RESOLUTION OF RACEMIC PANTOLACTONE WITH A NOVEL FUNGAL ENZYME, LACTONOHYDROLASE
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DOI：
10.1007/bf00166911
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发表时间：
1995-11-01
影响因子：
5
通讯作者：
SHIMIZU, S
中科院分区：
文献类型：
--
作者：
KATAOKA, M;SHIMIZU, K;SHIMIZU, S
报道了一种通过尖孢镰刀菌乳糖水解酶对D-泛内酯进行立体定向水解酶催化拆分外消旋潘托拉内酯的新工艺。F，尖孢子菌细胞催化外消旋潘托拉内酯的D-对映体的立体选择性水解。以135g/L的DL-泛内酯为底物，水解率为41%，得到光学纯度为90%对映体过量的泛酸(对映体过量为D-泛酸)。
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/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.