作者: Anika C. Jahns , Bernd H. A. Rehm
DOI: 10.1007/S10529-014-1735-7
关键词: Polyhydroxyalkanoates 、 Lipase 、 Glycerol 、 Candida antarctica 、 PHA synthase 、 Protein content 、 Biochemistry 、 Biology 、 Lipase b 、 Escherichia coli
摘要: Polyhydroxyalkanoate (PHA) beads, recombinantly produced in Escherichia coli, were functionalized to display lipase B from Candida antarctica as translational protein fusion. The respective beads characterized respect content, functionality, long term storage capacity and re-usability. direct fusion of the PHA synthase, PhaC, yielded active capable hydrolyzing glycerol tributyrate. Lipase showed stable activity over several weeks re-usability without loss function.