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

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

Research output: Contribution to journalArticleResearchpeer-review

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.

LanguageEnglish
Pages472-476
Number of pages5
JournalEnzyme and Microbial Technology
Volume31
Issue number4
DOIs
Publication statusPublished - 2 Sep 2002

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Enantioselectivity
Lipases
Lipase
Substrates
Esters
Enzymes
Bacilli
Fatty acids
Bacillus
Plasmids
Fatty Acids
Genes
Temperature

Cite this

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Biochemical characterization of a recombinant thermoalkalophilic lipase and assessment of its substrate enantioselectivity. / Sunna, Anwar; Hunter, Luke; Hutton, Craig A.; Bergquist, Peter L.

In: Enzyme and Microbial Technology, Vol. 31, No. 4, 02.09.2002, p. 472-476.

Research output: Contribution to journalArticleResearchpeer-review

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