Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: Sequence analysis and over-expression in Escherichia coli

Rinat N. Alon, David L. Gutnick*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

The est gene encoding an esterase from Acinetobacter lwoffii RAG-1 was cloned into E. coli under the control of the PL promoter of the phage λ. The N-terminal sequence of the first 20 amino acids of the heterologous expressed esterase corresponded to that obtained from the nucleotide sequence. Antibodies prepared against the over-expressed recombinant esterase in E.coli were used to locate the enzyme primarily in the membrane fractions of A. lwoffiiRAG-1. Comparison with homologous proteins from both eukaryotic and prokaryotic organisms suggest that the RAG-1 esterase exhibits sequence motifs characteristic of both serine proteases and of lipases.

Original languageEnglish
Pages (from-to)275-280
Number of pages6
JournalFEMS Microbiology Letters
Volume112
Issue number3
DOIs
StatePublished - 15 Sep 1993

Keywords

  • Acinetobacter lwoffi
  • Escherichia coli
  • Esterase
  • Lipase
  • Overexpression
  • Serine protease

Fingerprint

Dive into the research topics of 'Esterase from the oil-degrading Acinetobacter lwoffii RAG-1: Sequence analysis and over-expression in Escherichia coli'. Together they form a unique fingerprint.

Cite this