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Immobilization of Active Lipase B From Candida Antarctica on the Surface of Polyhydroxyalkanoate Inclusions

Anika C Jahns, Bernd H A Rehm

Biotechnol Lett. 2015 Apr;37(4):831-5.

PMID: 25407130

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP9001621-D Lipase from Candida antarctica Lipase from Candida antarctica 9001-62-1 Price
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