Departamento de Biocatálisis. Instituto de Catálisis - CSIC, Campus UAM-CSIC Cantoblanco, 28049 Madrid Spain.
Enzyme Microb Technol. 2011 Jun 10;49(1):72-8. doi: 10.1016/j.enzmictec.2011.03.002. Epub 2011 Mar 16.
Two commercial porous styrene-divinylbenzene beads (Diaion HP20LX and MCI GEL CHP20P) have been evaluated as supports to immobilize lipase B from Candida antarctica (CALB). MCI GEL CHP20P rapidly immobilized the enzyme, permitting a very high loading capacity: around 110mgCALB/wetg of support compared to the 50mg obtained using decaoctyl Sepabeads. Although enzyme specificity of the enzyme immobilized on different supports was quite altered by the support used in the immobilization, specific activity of the enzyme immobilized on MCI GEL CHP20P was always higher than those found using decaoctyl Sepabeads for all assayed substrates. Thus, a CALB biocatalyst having 3-8 folds (depending on the substrate) higher activity/wet gram of support than the commercial Novozym 435 was obtained. Half-live of CAL-Diaion HP20LX at 60°C was 2-3 higher than the one of Novozym 435, it was 30-40 higher in the presence of 50% acetonitrile and it was around 100 folds greater in the presence of 10M hydrogen peroxide. Results indicate that styrene-divinylbenzene supports may be promising alternatives as supports to immobilize CALB.
两种商业用多孔苯乙烯-二乙烯基苯珠（Diaion HP20LX 和 MCI GEL CHP20P）被评估为固定南极假丝酵母脂肪酶 B（CALB）的载体。MCI GEL CHP20P 迅速固定了酶，使其具有非常高的负载能力：与使用十辛基 Sepabeads 获得的 50mg 相比，约为 110mgCALB/湿 g 载体。尽管不同载体固定的酶的酶特异性受到载体的很大影响，但固定在 MCI GEL CHP20P 上的酶的比活性始终高于使用十辛基 Sepabeads 时所有测定的底物。因此，获得了一种比 Novozym 435 高 3-8 倍（取决于底物）活性/wet 克载体的 CALB 生物催化剂。CAL-Diaion HP20LX 在 60°C 下的半衰期比 Novozym 435 高 2-3 倍，在 50%乙腈存在下高 30-40 倍，在 10M 过氧化氢存在下高 100 倍左右。结果表明，苯乙烯-二乙烯基苯载体可能是固定 CALB 的有前途的替代载体。
