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

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. © 2002 Elsevier Science Inc. All rights reserved.