Tver State Technical University, A.Nikitin emb., 22, Tver, 170026, Russia.
Faraday Discuss. 2017 Sep 21;202:303-314. doi: 10.1039/c7fd00042a.
During this work, we studied the possibility of glucose oxidase (GOx) covalent immobilization on a modified inorganic support. A series of GOx-based biocatalysts was synthesized by crosslinking the enzyme to a surface of modified silica or alumina. Polyelectrolyte layers were used as modifiers for the silica and alumina surfaces. These layers promote tight binding of the GOx to the support. The biocatalyst's activity and stability were studied using an oxidation reaction of d-glucose to d-gluconic acid. It was found that GOx immobilized on the modified SiO using glutardialdehyde as a crosslinking agent was the most active and stable catalytic system, showing an 85% yield of gluconic acid. A study of the synthesized biocatalyst structure using FTIR spectroscopy showed that the enzyme was covalently crosslinked to the surface of an inorganic support modified with chitosan and glutardialdehyde. In the case of SiO, the quantity of the immobilized enzyme was higher than in the case of AlO.
在这项工作中，我们研究了葡萄糖氧化酶（GOx）共价固定在改性无机载体上的可能性。通过将酶交联到改性二氧化硅或氧化铝的表面，合成了一系列基于 GOx 的生物催化剂。聚电解质层被用作二氧化硅和氧化铝表面的改性剂。这些层促进了 GOx 与载体的紧密结合。使用 d-葡萄糖氧化反应研究了生物催化剂的活性和稳定性，生成 d-葡萄糖二酸。结果表明，使用戊二醛作为交联剂固定在改性 SiO 上的 GOx 是最活跃和稳定的催化体系，葡萄糖酸的产率为 85%。使用傅里叶变换红外光谱研究合成生物催化剂的结构表明，酶与壳聚糖和戊二醛改性的无机载体表面发生了共价交联。在 SiO 的情况下，固定化酶的量高于 AlO 的情况。
