Biochemical characterization of a recombinant thermoalkalophilic lipase and assessment of its substrate enantioselectivity

Anwar Sunna, Luke Hunter, Craig A. Hutton, Peter L. Bergquist*

*Corresponding author for this work

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

An expression plasmid encoding the lipase gene of the thermophilic lipase, LipA, of Bacillus sp. Tp10A.1 was constructed. The biochemical properties of the recombinant enzyme and its substrate enantioselectivity were studied. The optimum temperature and pH of the purified lipase is 60°C and 8.0, respectively. The purified enzyme was a true lipase with preference towards p-nitrophenyl esters with longer fatty acids. Purified recombinant LipA showed high enantioselectivity on selected racemic ester substrates.

Original languageEnglish
Pages (from-to)472-476
Number of pages5
JournalEnzyme and Microbial Technology
Volume31
Issue number4
DOIs
Publication statusPublished - 2 Sep 2002

Fingerprint Dive into the research topics of 'Biochemical characterization of a recombinant thermoalkalophilic lipase and assessment of its substrate enantioselectivity'. Together they form a unique fingerprint.

  • Cite this