Department of Immunology, Microbiology and Physiological Chemistry, Faculty of Biotechnology and Animal Husbandry, West Pomeranian University of Technology, Szczecin, 45 Piastów Avenue, 71-311, Szczecin, Poland.
Faculty of Chemical Technology and Engineering, Institute of Chemical Engineering and Environmental Protection Processes, West Pomeranian University of Technology, Szczecin, 42 Piastów Avenue, 71-065, Szczecin, Poland.
Appl Biochem Biotechnol. 2019 Jan;187(1):176-193. doi: 10.1007/s12010-018-2816-1. Epub 2018 Jun 18.
Bacterial cellulose spheres subjected to amination and inlaid modification with superparamagnetic molecules were analyzed with regard to possibility of their application as an immobilization carrier of Lecitase® Ultra (LU) enzyme. The starting point to obtain the carrier was synthesis of bacterial cellulose spheres performed in shaking cultures of Komagataeibacter xylinus. These spheres were subsequently subjected to a multi-stage modification to increase the efficiency of the immobilization process and to separate product from the reaction medium. Maximal yield of Lecitase® Ultra immobilization equaled 70%. It was also found that immobilization process did not affect the pH and LU temperature optimum. Moreover, immobilized enzyme exhibited similar temperature stability profile as its native form. The immobilization process did not significantly affect the enzyme K value. The immobilized enzyme retained over 70% of its initial activity after 8 cycles of use. The immobilized enzyme displayed good storage stability and retained 80% of its initial activity after 4 weeks at 4 °C. The potential application of such modified cellulose-based carrier may be correlated with lower costs of process thanks to higher enzyme's reusability in comparison to unbound enzyme. Moreover, data presented in the current study may serve as proof of a concept of cellulose-based carrier utilization for immobilization of enzymes other than LU and of high industrial importance.
经氨化和超顺磁性分子嵌入修饰的细菌纤维素球，可作为 Lecitase® Ultra（LU）酶的固定化载体。研究从摇瓶培养的木醋杆菌合成细菌纤维素球开始，然后对这些球进行多步修饰，以提高固定化效率并将产物与反应介质分离。最大的 Lecitase® Ultra 固定化收率为 70%。还发现固定化过程不影响 pH 值和 LU 最适温度。此外，固定化酶表现出与其天然形式相似的温度稳定性。固定化过程对酶的 K 值没有显著影响。固定化酶在使用 8 个周期后仍保留超过 70%的初始活性。固定化酶在 4°C 下储存 4 周后仍保留 80%的初始活性。这种改性纤维素载体的潜在应用可能与更高的酶重复使用率相关，从而降低了成本，与未结合的酶相比，具有更高的酶的重复使用性。此外，当前研究中的数据可作为纤维素载体用于固定化除 LU 以外的其他具有重要工业价值的酶的概念验证。
