The unexpected esterase activity of an industrial glutaryl acylase was investigated. Glutaryl esters of a series of primary and secondary alcohols as well as of phenols were all efficiently hydrolyzed, the only exception being the sterically hindered glutarate of thymol. The enantioselectivities of the acylase, which were evaluated with three of these substrates, were quite low (E values ranging between 1.9 and 7.2), but were significantly improved by substrate and/or solvent engineering. Enantiomerically enriched hydrolyzed alcohols and unreacted glutarates can be easily separated by selective extraction, thus avoiding chromatographic steps.
Enantioselective esterase activity of an industrial glutaryl acylase
Monti D;Riva S
2005
Abstract
The unexpected esterase activity of an industrial glutaryl acylase was investigated. Glutaryl esters of a series of primary and secondary alcohols as well as of phenols were all efficiently hydrolyzed, the only exception being the sterically hindered glutarate of thymol. The enantioselectivities of the acylase, which were evaluated with three of these substrates, were quite low (E values ranging between 1.9 and 7.2), but were significantly improved by substrate and/or solvent engineering. Enantiomerically enriched hydrolyzed alcohols and unreacted glutarates can be easily separated by selective extraction, thus avoiding chromatographic steps.| File | Dimensione | Formato | |
|---|---|---|---|
|
prod_17388-doc_11083.pdf
non disponibili
Descrizione: Articolo pubblicato
Dimensione
124.56 kB
Formato
Adobe PDF
|
124.56 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
