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.

包含亲脂性和亲水性纳米空间以模仿脂质双层的新型有机-无机杂化多孔材料（KCS-2）被用作谷氨酸脱羧酶（GADβ）的固定化载体和反应促进剂。在评价GADβ在KCS-2上的吸附时，发现固定化量比在无孔二氧化硅上的固着量高大约四倍，并且观察到与中孔二氧化硅相当的吸附性。通过将l脱羧而生成γ-氨基丁酸（GABA）-谷氨酸使用这些固定化酶，发现GADβ-KCS-2复合物的酶活性明显高于游离酶。相反，更常见的GADβ-介孔二氧化硅复合材料的活性下降。此外，在宽温度范围内，GADβ–KCS-2复合物的酶促活性优于未固定化的游离酶和无定形物质本身。因此，这些发现表明，在这种条件下，KCS-2的两亲性纳米空间适合作为稳定的酶固定场和反应加速场。另外，根据GABA产生检查了固定化酶的耐久性，使用KCS-2在10个循环后观察到约20％的活性保留。