RT Journal Article
T1 Poly-3-Hydroxybutyrate Functionalization with BioF-Tagged Recombinant Proteins
A1 Bello-Gil, Daniel
A1 Maestro García-Donas, María Beatriz
A1 Fonseca, Jennifer
A1 Dinjaski, Nina
A1 Prieto, Auxiliadora
A1 Sanz, Jesús
AB Polyhydroxyalkanoates (PHAs) are biodegradable polyesters that accumulate in the cytoplasm of certain bacteria. One promising biotechnological application utilizes these biopolymers as supports for protein immobilization. Here, the PHA-binding domain of the Pseudomonas putida KT2440 PhaF phasin (BioF polypeptide) was investigated as an affinity tag for the in vitro functionalization of poly-3-hydroxybutyrate (PHB) particles with recombinant proteins, namely, full-length PhaF and two fusion proteins tagged to BioF (BioF–C-LytA and BioF–β-galactosidase, containing the choline-binding module C-LytA and the β-galactosidase enzyme, respectively). The protein-biopolyester interaction was strong and stable at a wide range of pHs and temperatures, and the bound protein was highly protected from self-degradation, while the binding strength could be modulated by coating with amphiphilic compounds. Finally, BioF–β-galactosidase displayed very stable enzymatic activity after several continuous activity-plus-washing cycles when immobilized in a minibioreactor. Our results demonstrate the potentialities of PHA and the BioF tag for the construction of novel bioactive materials.
SN 0099-2240
YR 2018
FD 2018
LK https://hdl.handle.net/20.500.14352/92515.2
UL https://hdl.handle.net/20.500.14352/92515.2
LA eng
NO Bello-Gil DMaestro BFonseca J, Dinjaski NPrieto MA, Sanz JM 2018. Poly-3-Hydroxybutyrate Functionalization with BioF-Tagged Recombinant Proteins. Appl Environ Microbiol 84:e02595-17.https://doi.org/10.1128/AEM.02595-17
NO Ministerio de Economía y Competitividad (España)
NO Comunidad de Madrid
DS Docta Complutense
RD 9 abr 2025