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Applied and Environmental Microbiology, June 2007, p. 3838-3844, Vol. 73, No. 12
0099-2240/07/$08.00+0     doi:10.1128/AEM.00097-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Hexadecane and Tween 80 Stimulate Lipase Production in Burkholderia glumae by Different Mechanisms

Bouke K. H. L. Boekema,¹ Anke Beselin,^2, Michael Breuer,³ Bernhard Hauer,³ Margot Koster,¹ Frank Rosenau,² Karl-Erich Jaeger,² and Jan Tommassen^1*

Department of Molecular Microbiology and Institute for Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands,¹ Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, 52426 Jülich, Germany,² Fine Chemicals & Biocatalysis Research, BASF AG, 67056 Ludwigshafen, Germany³

Received 15 January 2007/ Accepted 23 April 2007

Burkholderia glumae strain PG1 produces a lipase of biotechnological relevance. Lipase production by this strain and its derivative LU8093, which was obtained through classical strain improvement, was investigated under different conditions. When 10% hexadecane was included in the growth medium, lipolytic activity in both strains could be increased 7-fold after 24 h of growth. Hexadecane also stimulated lipase production in a strain containing the lipase gene fused to the tac promoter, indicating that hexadecane did not affect lipase gene expression at the transcriptional level, which was confirmed using lipA-gfp reporter constructs. Instead, hexadecane appeared to enhance lipase secretion, since the amounts of lipase in the culture supernatant increased in the presence of hexadecane, with a concomitant decrease in the cells, even when protein synthesis was inhibited with chloramphenicol. In the presence of olive oil as a carbon source, nonionic detergents, such as Tween 80, increased extracellular lipase activity twofold. Like hexadecane, Tween 80 appeared to stimulate lipase secretion, although in a more disruptive manner, since other, normally nonsecreted proteins were found in the culture supernatant. Additionally, like olive oil, Tween 80 was found to induce lipase gene expression in strain PG1 in medium containing sucrose as a carbon source but not in glucose-containing medium, suggesting that lipase gene expression is prone to catabolite repression. In contrast, lipase production in the lipase-overproducing strain LU8093 was independent of the presence of an inducer and was not inhibited by glucose. In conclusion, hexadecane and Tween 80 enhance lipase production in B. glumae, and they act via different mechanisms.

Published ahead of print on 27 April 2007.

Present address: Lilly Deutschland GmbH, 61350 Bad Homburg v.d. Höhe, Germany.