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