engleski

The investigation of the stability of 2- deoxyribose-5-phosphate aldolase

The sequential aldol condensation catalyzed by 2- deoxyribose-5-phosphate aldolase (DERA, EC 4.1.2.4) is one of the most promising routes for the synthesis of statin side chains. DERA is the only aldolase known to stereoselectively accept three aldehydes in a series of sequential steps during an aldol condensation reaction without any cofactors (1). By using inexpensive, achiral acetaldehyde and chloroacetaldehyde as substrates the reaction catalyzed by DERA gives lactols containing two chiral centers of the final statin side chain with excellent stereopurity and high yield in a single step. Since the enzyme activity decreases when exposed to an unfavorable environment, the enzyme stability is a crucial factor to determine whether the application of biocatalysis will be commercially successful (2). Therefore, the effects of temperature and different buffers at various pH on DERA activity and stability were investigated as well as the influence of different chloroacetaldehyde and acetaldehyde concentrations. Based on the acquired experimental data the optimal conditions for the aldol condensation catalyzed by DERA were obtained.

2-deoxyribose-5-phosphate aldolase ; stability ; activity

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