ملخص
The performance of (S)-oxynitrilase from Hevea brasiliensis (HbHNL) has been investigated with several α- and β-substituted alkyl or alkoxy aldehydes and the results have been compared to the data previously obtained with the (R)-specific enzyme from almonds (PaHNL). With both enzymes there was no chiral discrimination between the enantiomers of the racemic substrates, therefore this reaction cannot be used as a preparative method to achieve both the kinetic resolution of the starting racemic aldehyde and the production of diastereomerically pure (or enriched) cyanohydrins. Additionally, in comparison with the (R)-PaHNL the (S)-selective enzyme from Hevea gave products with higher de, but was more negatively effected by oxygenated substituents.
اللغة الأصلية | English |
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الصفحات (من إلى) | 2979-2983 |
عدد الصفحات | 5 |
دورية | Tetrahedron |
مستوى الصوت | 58 |
رقم الإصدار | 15 |
المعرِّفات الرقمية للأشياء | |
حالة النشر | Published - أبريل 8 2002 |
منشور خارجيًا | نعم |
ASJC Scopus subject areas
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