Cloning and expression in Escherichia coli of apolyurethane-degrading enzyme from Pseudomonasfluorescens
作者： Rodney E Vega , Tina Main , Gary T Howard
DOI: 10.1016/S0964-8305(98)00068-7
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摘要: Abstract A polyester polyurethane (PU)-degrading enzyme, PU esterase, derived from Pseudomonas fluorescens, a bacterium that utilizes as the sole carbon source,was purified to homogeneity indicated by sodium dodecyl sulfate-polyacrylamide gelelectrophoresis. This enzyme was soluble, extracellular protein with molecular mass of 48 kDa and inhibited phenylmethylsulfonylfluoride (PMSF). genomic library Ps.fluorescens constructed using Escherichia coli bacteriophage l vector lZAPII. recombinant phage exhibiting activity against Impranil DLN isolated. The geneencoding polyurethanase (PUase) subcloned into plasmid expression vectorpT7-6 expressed in E. coli. Upon expression, PUase secreted host,displayed esterase which PMSF, vivo 35S-methionine labeling gene product encoded open reading frame clone insertrevealed single polypeptide kDa.
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