Purification and characterization of a soluble polyurethane degrading enzyme from Comamonas acidovorans
Purification and characterization of a soluble polyurethane degrading enzyme from Comamonas acidovorans
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DOI：
10.1016/s0964-8305(98)00066-3
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发表时间：
1999-01-01
影响因子：
4.8
通讯作者：
Howard, GT
中科院分区：
文献类型：
--
作者：
Allen, AB;Hilliard, NP;Howard, GT
对一种与聚酯型聚氨酯（PU）生物降解有关的可溶性酯酶进行了纯化，得到了电泳纯的酯酶，产率约为83%。该酶在非变性（ND-）和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）上均显示单一条带，表观分子量为42 kDa。以邻硝基苯乙酸为底物，该酶的稳态动力学参数Km和Vmax分别为51.5 mM和180 U mg（-1）。酯酶对热稳定，能被苯甲基磺酰氟（PMSF）和大豆胰蛋白酶抑制剂（STI）抑制。(C)1999 Elsevier Science Ltd.保留所有权利。
A soluble esterase involved in the biodegradation of polyester polyurethane (PU) was purified to apparent electrophoretic homogeneity in high yield, similar to 83%. The enzyme displayed a single band on both non-denaturing (ND-) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with an apparent molecular mass of 42 kDa. Using rho-nitrophenylacetate as the substrate, the enzyme displayed steady-state kinetic parameters K-m and V-max of 51.5 mM and 180 U mg(-1) respectively. Esterase activity was thermally stable and could be inhibited with phenylmethylsulfonylfluoride (PMSF) and soybean trypsin inhibitor (STI). (C) 1999 Elsevier Science Ltd. All rights reserved.