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Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

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Display of functionally active PHB depolymerase on Escherichia coli cell surface.

Tomohiro Hiraishi¹, Koichi Yamashita, Masafumi Sakono

¹Bioengineering Laboratory, RIKEN Advanced Science Institute, Wako-shi, Saitama, Japan. thiraish@riken.jp

Macromolecular Bioscience

|November 19, 2011

Summary

Researchers engineered E. coli to display polyhydroxyalkanoate (PHA) depolymerase (PhaZ(RpiT1)) on its surface. This whole-cell biocatalyst efficiently degrades PHA materials into valuable monomers.

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Area of Science:

Biotechnology and Metabolic Engineering
Enzyme Engineering and Biocatalysis
Polymer Science and Engineering

Background:

Polyhydroxyalkanoates (PHAs) are biodegradable polyesters with diverse applications.
Efficient enzymatic degradation of PHAs into valuable monomers is crucial for sustainable production.
Cell surface display technology offers a promising platform for whole-cell biocatalysts.

Purpose of the Study:

To engineer Escherichia coli (E. coli) for surface display of polyhydroxyalkanoate (PHA) depolymerase (PhaZ(RpiT1)).
To evaluate the enzymatic activity and stability of the displayed PHA depolymerase.
To assess the potential of engineered E. coli as a whole-cell biocatalyst for PHA degradation.

Main Methods:

Construction of a fusion protein between PhaZ(RpiT1) and OprI from Pseudomonas aeruginosa for cell surface anchoring.
Stable expression and surface localization of the fusion protein in E. coli JM109, verified by immunofluorescence microscopy.
Assessment of the catalytic activity of displayed PhaZ(RpiT1) on both soluble and insoluble PHA substrates.

Main Results:

Successful display of functional PhaZ(RpiT1) on the surface of E. coli JM109 cells.
The displayed enzyme retained its ability to cleave soluble substrates and adsorb to PHA surfaces.
Catalytic activity was maintained for the degradation of insoluble PHA materials, demonstrating potential as a whole-cell biocatalyst.

Conclusions:

Engineered E. coli displaying PhaZ(RpiT1) serves as an effective whole-cell biocatalyst for PHA degradation.
This approach facilitates the production of (R)-3-hydroxybutyrate monomers from insoluble PHA.
Cell surface display of PHA depolymerase offers a sustainable and efficient method for PHA valorization.