Covalent-bonded immobilization of lipase on poly(phenylene sulfide) dendrimers and their hydrolysis ability.
Covalent-bonded immobilization of lipase on poly(phenylene sulfide) dendrimers and their hydrolysis ability.
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DOI：
10.1021/bm050285d
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发表时间：
2005-08
影响因子：
6.2
通讯作者：
O. Yemul;T. Imae
中科院分区：
文献类型：
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作者：
O. Yemul;T. Imae
以碳二亚胺为偶联试剂，将洋葱伯克霍尔德菌脂肪酶共价固定在两种不同代数（2代和3代）的聚苯硫醚（PPS）树枝状大分子上。研究了PPS树枝状聚合物固定化酶催化橄榄油水解制备脂肪酸的活性。酶活性与酶负载成比例，并且对于G2和G3树枝状聚合物两者，在中等酶负载下获得最高回收活性。固定化提高了最适pH值，并导致温度范围扩大。酶的固定化与游离酶相比，提高了酶活力的热稳定性。该固定化酶作为分批水解橄榄油的生物催化剂，循环使用20次后仍保持80%左右的活性。在酶技术中，这种循环后的活性保留是非常有价值和强大的。树状大分子共价键合固定化脂肪酶在酶反应中的重要作用是由于树状大分子具有大量的末端功能基团，在保持活性酶在树状大分子表面的情况下，易于固定化多种脂肪酶。
Covalent-bonded immobilization of lipase from burkholderia cepacia onto two poly(phenylene sulfide) (PPS) dendrimers with different generations (two and three) was achieved using carbodiimide as a coupling reagent. The hydrolysis activity of olive oil to fatty acid was studied on enzyme-immobilized PPS dendrimers. Enzyme activity was proportional to the enzyme loading, and highest recovered activity was obtained at the medium enzyme loading for both G2 and G3 dendrimers. The immobilization improved the optimum pH and caused the temperature range to widen. Immobilization of enzyme has enhanced the thermal stability of enzyme activity in comparison with free enzyme. The immobilized enzyme as a biocatalyst for batch hydrolysis of olive oil retained 80 approximately 90% activity even after 20 times of recycling. This retention of activity after recycle is very valuable and powerful in enzyme technology. The present noteworthy and vital availability on enzyme reaction of the covalently bonded immobilized lipase on dendrimer came from the structure of dendrimer with a large number of functional terminal groups, which are easily available for immobilization of many lipases at the situation keeping reactive enzymes on the surface of dendrimer.