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Enzymology and Protein Engineering

Poly-3-Hydroxybutyrate Functionalization with BioF-Tagged Recombinant Proteins

Daniel Bello-Gil, Beatriz Maestro, Jennifer Fonseca, Nina Dinjaski, M. Auxiliadora Prieto, Jesús M. Sanz
Ning-Yi Zhou, Editor
Daniel Bello-Gil
aInstituto de Biología Molecular y Celular, Universidad Miguel Hernández, Elche, Spain
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Beatriz Maestro
aInstituto de Biología Molecular y Celular, Universidad Miguel Hernández, Elche, Spain
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Jennifer Fonseca
aInstituto de Biología Molecular y Celular, Universidad Miguel Hernández, Elche, Spain
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Nina Dinjaski
bCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CIB-CSIC), Madrid, Spain
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M. Auxiliadora Prieto
bCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CIB-CSIC), Madrid, Spain
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Jesús M. Sanz
aInstituto de Biología Molecular y Celular, Universidad Miguel Hernández, Elche, Spain
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  • ORCID record for Jesús M. Sanz
Ning-Yi Zhou
Shanghai Jiao Tong University
Roles: Editor
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DOI: 10.1128/AEM.02595-17
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ABSTRACT

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.

IMPORTANCE Our results confirm the biotechnological potential of the BioF affinity tag as a versatile tool for functionalizing PHA supports with recombinant proteins, leading to novel bioactive materials. The wide substrate range of the BioF tag presumably enables protein immobilization in vitro of virtually all natural PHAs as well as blends, copolymers, or artificial chemically modified derivatives with novel physicochemical properties. Moreover, the strength of protein adsorption may be easily modulated by varying the coating of the support, providing new perspectives for the engineering of bioactive materials that require a tight control of protein loading.

FOOTNOTES

    • Received 21 November 2017.
    • Accepted 27 November 2017.
    • Accepted manuscript posted online 1 December 2017.
  • Supplemental material for this article may be found at https://doi.org/10.1128/AEM.02595-17.

  • Copyright © 2018 American Society for Microbiology.

All Rights Reserved.

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Poly-3-Hydroxybutyrate Functionalization with BioF-Tagged Recombinant Proteins
Daniel Bello-Gil, Beatriz Maestro, Jennifer Fonseca, Nina Dinjaski, M. Auxiliadora Prieto, Jesús M. Sanz
Applied and Environmental Microbiology Jan 2018, 84 (4) e02595-17; DOI: 10.1128/AEM.02595-17

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Poly-3-Hydroxybutyrate Functionalization with BioF-Tagged Recombinant Proteins
Daniel Bello-Gil, Beatriz Maestro, Jennifer Fonseca, Nina Dinjaski, M. Auxiliadora Prieto, Jesús M. Sanz
Applied and Environmental Microbiology Jan 2018, 84 (4) e02595-17; DOI: 10.1128/AEM.02595-17
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KEYWORDS

PHB
phasins
affinity tag
protein immobilization
polyhydroxyalkanoates

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