Palmieri G, Giardina P, Desiderio B, Marzullo L, Giamberini M, Sannia G
Dipartimento di Chimica Organica e Biologica, Università degli Studi di Napoli Federico II, Italy.
Enzyme Microb Technol. 1994 Feb;16(2):151-8. doi: 10.1016/0141-0229(94)90078-7.
A new procedure was developed for enzyme immobilization by entrapment in copper alginate gel. The mechanical properties of the copper alginate gel were characterized and compared with those of the most widely used calcium alginate. The system was applied to the immobilization of a fungal phenol oxidase. Optimal conditions for enzyme immobilization were set up: the system immobilized 85% of the enzyme, and the remaining 15% was recovered in the aqueous immobilization medium. The stability and activity of the immobilized enzyme were studied. After immobilization, the enzyme was active in a wider pH range, the temperature of its optimal activity was shifted to lower values, and the possibility of storage at 4 degrees C was greatly improved. The immobilized enzyme generally increased the rate of oxidation of various substrates. The results indicate a potential use of this system for the construction of bioreactors to be used in the detoxification of polluted waste waters.
开发了一种通过包埋于海藻酸铜凝胶中来固定化酶的新方法。对海藻酸铜凝胶的机械性能进行了表征，并与使用最广泛的海藻酸钙的机械性能进行了比较。该系统应用于固定化一种真菌酚氧化酶。确定了最佳的酶固定化条件：该系统固定了85%的酶，其余15%在水相固定化介质中回收。研究了固定化酶的稳定性和活性。固定化后，酶在更宽的pH范围内具有活性，其最佳活性温度向更低的值偏移，并且在4℃下储存的可能性大大提高。固定化酶总体上提高了各种底物的氧化速率。结果表明该系统在构建用于处理受污染废水解毒的生物反应器方面具有潜在用途。
