Purification and characterization of a solublepolyurethane degrading enzyme from Comamonasacidovorans

A soluble esterase involved in the biodegradation of polyester polyurethane (PU) waspurified to apparent electrophoretic homogeneity in high yield, 83%. The enzyme displayed asingle band on both non-denaturing (ND-) and sodium dodecyl sulfate-polyacrylamide gelelectrophoresis (SDS-PAGE) with an apparent molecular mass of 42 kDa. Using ρ-nitrophenylacetate as the substrate, the enzyme displayed steady-state kinetic parameters Km and Vmax of 51.5 mM and 180 U mg−1 respectively. Esteraseactivity was thermally stable and could be inhibited with phenylmethylsulfonylfluoride (PMSF)and soybean trypsin inhibitor (STI). © 1999 Elsevier Science Ltd. All rights reserved.