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

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

doi:10.1016/S0141-0229(02)00133-3

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 journal › Article › peer-review

32 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 language	English
Pages (from-to)	472-476
Number of pages	5
Journal	Enzyme and Microbial Technology
Volume	31
Issue number	4
DOIs	https://doi.org/10.1016/S0141-0229(02)00133-3
Publication status	Published - 2 Sep 2002

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AB - 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.

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

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