title: Immobilization of active lipase B from Candida antarctica on the surface of polyhydroxyalkanoate inclusions.
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.
authors.affiliation: Institute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North, 4442, New Zealand, anika.jahns@medbio.umu.se.
authors.forename: Anika C
authors.initials: AC
authors.lastname: Jahns
authors.forename: Bernd H A
authors.initials: BH
authors.lastname: Rehm
mesh_terms: D000217:Acyltransferases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D002175:Candida / Q000201:enzymology*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006868:Hydrolysis; D008049:Lipase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D054813:Polyhydroxyalkanoates / Q000276:immunology* / Q000378:metabolism; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D014280:Triglycerides / Q000378:metabolism
chemical_list: D004800:Enzymes, Immobilized; D054813:Polyhydroxyalkanoates; D011993:Recombinant Fusion Proteins; D014280:Triglycerides; D000217:Acyltransferases; C077225:poly(3-hydroxyalkanoic acid) synthase; D008049:Lipase; C005830:tributyrin