Enzymatic transesterification of monosaccharides and amino acid esters in organic solvents
β Scribed by Oh-Jin Park; Hyun Gyu Park; Ji-Won Yang
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 413 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0141-5492
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β¦ Synopsis
Lipases and proteases from different sources were screened for their ability to catalyze the transesterification of glucose and activated N-blocked phen fs lalanine. A commercial 8 rotease from Bacillus licheniformis was found to be most e ective for this purpose.
n a basis of "C-NMR analysis, .glucose was acylated at the C-6 position. The enzyme showed a broad substrate specificity toward various monosaccharides.
π SIMILAR VOLUMES
An expedient synthesis of homochiral N-protected (R)and (S)-3-hydroxy+pentenylamines (1 and 2) has been accomplished via the enzymatic resolution of the racemic 1 and 2 mediated by immobilized lipase in pcntane.