Biochemical Processing and Biomaterial Research Laboratory, Faculty of Arts and Sciences, Gazi University, Teknik Okullar, 06500, Ankara, Turkey.
Bioprocess Biosyst Eng. 2011 Aug;34(6):735-46. doi: 10.1007/s00449-011-0523-1. Epub 2011 Feb 19.
Fibrous poly(styrene-b-glycidylmethacrylate) brushes were grafted on poly(styrene-divinylbenzene) (P(S-DVB)) beads using surface-initiated atom transfer radical polymerization. Tetraethyldiethylenetriamine (TEDETA) ligand was incorporated on P(GMA) block. The ligand attached beads were used for reversible immobilization of lipase. The influences of pH, ionic strength, and initial lipase concentration on the immobilization capacities of the beads have been investigated. Lipase adsorption capacity of the beads was about 78.1 mg/g beads at pH 6.0. The Km value for immobilized lipase was about 2.1-fold higher than that of free enzyme. The thermal, and storage stability of the immobilized lipase also was increased compared to the native lipase. It was observed that the same support enzyme could be repeatedly used for immobilization of lipase after regeneration without significant loss in adsorption capacity or enzyme activity. A lipase from Mucor miehei immobilized on styrene-divinylbenzene copolymer was used to catalyze the direct esterification of butyl alcohol and butyric acid.
纤维状聚（苯乙烯-甲基丙烯酸缩水甘油酯）刷通过表面引发原子转移自由基聚合接枝到聚苯乙烯-二乙烯基苯（P（S-DVB））珠上。四乙二胺四乙酸（TEDETA）配体被掺入 P（GMA）嵌段中。附着配体的珠子被用于脂肪酶的可逆固定化。考察了 pH 值、离子强度和初始脂肪酶浓度对珠子固定化容量的影响。在 pH 6.0 时，珠子的脂肪酶吸附容量约为 78.1 mg/g 珠子。固定化脂肪酶的 Km 值比游离酶高约 2.1 倍。与天然脂肪酶相比，固定化脂肪酶的热稳定性和储存稳定性也有所提高。观察到，经过再生后，相同的载体酶可以重复用于脂肪酶的固定化，而不会显著损失吸附容量或酶活性。米黑毛霉来源的脂肪酶固定在苯乙烯-二乙烯基苯共聚物上，用于催化丁醇和丁酸的直接酯化反应。
