Purification and characterization of a soluble polyurethane degrading enzyme from Comamonas acidovorans

被引:39
作者
Allen, AB
Hilliard, NP
Howard, GT [1 ]
机构
[1] SE Louisiana Univ, Dept Biol Sci, Hammond, LA 70402 USA
[2] SE Louisiana Univ, Dept Chem & Phys, Hammond, LA 70402 USA
关键词
comamonas acidovorans; polyurethane degradation; enzyme purification;
D O I
10.1016/S0964-8305(98)00066-3
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:37 / 41
页数:5
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