Efficient production of γ-aminobutyric acid by glutamate decarboxylase immobilized on an amphiphilic organic-inorganic hybrid porous material.

A novel organic-inorganic hybrid porous material (KCS-2), containing both lipophilic and hydrophilic nanospaces to mimic a lipid bilayer, was utilized as an immobilization support and reaction accelerator for glutamate decarboxylase (GADβ). Upon evaluation of the adsorption of GADβ on KCS-2, the amount of immobilization was found to be approximately four times higher than that on non-porous silica, and a comparable adsorbability to mesoporous silica was observed. Following γ-aminobutyric acid (GABA) production by the decarboxylation of l-glutamic acid using these immobilized enzymes, the enzymatic activity of the GADβ-KCS-2 composite was found to be significantly higher than that of the free enzyme. In contrast, the activity of the more common GADβ-mesoporous silica composite decreased. Furthermore, the enzymatic activity of the GADβ-KCS-2 composite was superior to those of the un-immobilized free enzyme and the amorphous material itself over a wide temperature range. Thereby, these findings suggest that the amphiphilic nanospace of KCS-2 is suitable as a stable enzyme immobilization field and reaction acceleration field under such conditions. In addition, the durability of the immobilized enzyme was examined in terms of GABA production, with approximately 20% activity retention being observed after 10 cycles using KCS-2. Such durability was not observed for the non-porous silica material due to enzyme desorption.