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

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-usabi...

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Bibliographic Details
Published in:Biotechnology Letters
Main Authors: Jahns, Anika C., Rehm, Bernd H.A.
Format: Article in Journal/Newspaper
Language:English
Published: Springer Netherlands 2015
Subjects:
Environmental Biotechnology not elsewhere classified
Antarc*
Antarctica
Online Access:http://hdl.handle.net/10072/342769
https://doi.org/10.1007/s10529-014-1735-7
Description
Summary: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. No Full Text

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