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Immobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions

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Abstract

Polyhydroxyalkanoate (PHA) beads, recombinantly produced in Escherichia coli, were functionalized to display lipase B from Candida antarctica as translational protein fusion. The respective beads were characterized in respect to protein content, functionality, long term storage capacity and re-usability. The direct fusion of the PHA synthase, PhaC, to lipase B yielded active PHA lipase beads capable of hydrolyzing glycerol tributyrate. Lipase B beads showed stable activity over several weeks and re-usability without loss of function.

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Acknowledgments

This work was funded by PolyBatics Ltd.

Conflict of interest

Bernd Rehm is Chief Science Officer as well as shareholder of Polybatics Ltd.

Supporting information

Supplementary Table 1—Bacterial strains, plasmids and oligonucleotides used in this study.

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Correspondence to Bernd H. A. Rehm.

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Jahns, A.C., Rehm, B.H.A. Immobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions. Biotechnol Lett 37, 831–835 (2015). https://doi.org/10.1007/s10529-014-1735-7

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  • DOI: https://doi.org/10.1007/s10529-014-1735-7

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