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Open Access Highly Accessed Research article

Mechanism of acetaldehyde-induced deactivation of microbial lipases

Benjamin Franken13, Thorsten Eggert2, Karl E Jaeger1 and Martina Pohl14*

Author Affiliations

1 Institute of Molecular Enzyme Technology, Heinrich-Heine University Düsseldorf, Forschungszentrum Jülich GmbH, D-52426 Jülich, Germany

2 evocatal GmbH, Merowinger Platz 1a, D-40225 Düsseldorf, Germany

3 QIAGEN GmbH, QIAGEN Straße 1, D-40724, Germany

4 Institute of Bio- and Geosciences, IBG-1: Biotechnology, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany

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BMC Biochemistry 2011, 12:10  doi:10.1186/1471-2091-12-10

Published: 22 February 2011

Additional files

Additional file 1:

Table S1: Predicted pKa-values of solvent accessible lysine ε-amino groups derived from all available lipase protein structures.

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Additional file 2:

Figure S1: Tributyrine plate assay of BSL-B wild type and BSL-B point variants. Tributyrine plate assay of BSL-B wild type as well as BSL-B point variants in which each lysine residue is substituted by alanine and arginine, respectively. -: E. coli BL21(DE3) carrying the empty vector pET19b. WT: E. coli BL21(DE3) expressing BSL-B wild type enzyme (pET19b + lipB). K X A/R: E. coli BL21(DE3) expressing BSL-B in which the lysine residue (K) at position X is substituted with alanine (A) or arginine (R).

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Additional file 3:

Table S2: Periodically measured DLS data of differently concentrated BSL-B samples.

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Additional file 4:

Table S3: PCR Primers QuikChange-PCR-primer sequences for site-directed mutagenesis of each lysine residue in BSL-B for alanine and arginine, respectively. Each primer pair (e.g. lipB-K25R-fw und lipB-K25A-fw) differs only in the mutagenesis sequence (bold and underlined).

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