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Title of article :
Biochemical characterization of a recombinant thermoalkalophilic lipase and assessment of its substrate enantioselectivity
Author/Authors :
Anwar Sunna، نويسنده , , Luke Hunter، نويسنده , , Craig A Hutton، نويسنده , , Peter L. Bergquist، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2002
Pages :
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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.
Keywords :
Substrate enantioselectivity , Thermostable lipase , Thermophilic Bacillus
Journal title :
Enzyme and Microbial Technology
Serial Year :
Link To Document :