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Immobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions
- Jahns, Anika C., Rehm, Bernd H. A.
- Biotechnology letters 2015 v.37 no.4 pp. 831-835
- Escherichia coli, Pseudozyma antarctica, glycerol, polyhydroxyalkanoates, protein content
- 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.