engleski

Activation agent optimization in aldolase immobilization on mesoporous silica

In the field of pharmaceutical synthesis one of the most researched and utilized reaction is the synthesis of statins, drugs used for lowering cholesterol levels in blood. Important statin side-chain precursor with two optically active centers can be produced by double aldol addition catalyzed by 2-deoxyribose-5-phosphate aldolase (DERA, EC 4.1.2.4) (Figure 1) [1]. While this reaction offers a lot of benefits associated with enzyme-catalyzed reactions, its main drawback is the enzyme inactivation due to the presence of high concentrations of both substrate and reaction intermediates. One of the methods to successfully combat this issue is enzyme immobilization which often leads to increased operational stability [2]. The aim of this work was to immobilize aldolase on mesoporous silica by covalent bonding with benzoquinone. Mesoporous silica was synthesized using the sol-gel method and functionalized with 3-aminopropyltriethoxysilane. Four different concentrations of benzoquinone were used for surface activation. In addition, the influence of temperature on the immobilization process was examined. In order to determine the optimal activation agent concentration and temperature, the success of immobilization was followed by measuring retained activity, stability and efficiency of the immobilized biocatalyst.

Aldolase ; Immobilization ; Mesoporous silica

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