Molecular Characterization of Polyurethanase Genes and Proteins from Pseudomonas.
Abstract
Our laboratory is studying the polyurethanase enzymes and genes that encode them from three species of Pseudomonas. We have purified and characterized five polyurethane hydrolyzing proteins and cloned four polyurethanase genes, in which two have been sequenced. Nucleotide sequencing of the polyurethanase genes revealed that the deduced polypeptide sequence contains a serine-hydrolase consensus sequence GXSXG. The polypeptides lacked an N-terminal signal peptide, but did contain a short region toward the C-terminus that has been observed in secreted. The most closely related proteins to the polyurethanases had amino acid sequences homologies of 70% for four lipases from P. fluorescens and 51% for lipases from Serratia marcescens. Northern blot analysis revealed that the polyurethanase genes are constitutively expressed. The results obtained from this study has yielded valuable information that is essential for an understanding of the biochemical and genetic properties of bacterial polyurethanases and how these properties may be utilized to improve polyurethane degradation. The study has a potentially major impact on understanding mechanisms by which enzymes degrade polyurethane.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 14, 1999
- Accession Number
- ADA365632
Entities
People
- Gary T. Howard
Organizations
- Southeastern Louisiana University