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Polyhydroyxalkanoate synthase fusions as a strategy for oriented enzyme immobilisation
David O Hooks1, Mark Venning-Slater2, Jinping Du3
1Institute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. d.o.hooks@massey.ac.nz.
Molecules (Basel, Switzerland)
|June 26, 2014
Summary
Polyhydroxyalkanoate (PHA) granules, produced by bacteria, can be engineered to immobilize enzymes. This novel method offers enhanced enzyme activity and product yields for biocatalysis.
Area of Science:
- Biotechnology
- Biochemistry
- Synthetic Biology
Background:
- Polyhydroxyalkanoates (PHAs) are bacterial carbon storage polymers.
- PHA granules are protein-coated inclusions, including PHA synthase (PhaC).
- PHA synthase facilitates PHA granule formation and can be genetically engineered.
Purpose of the Study:
- To review the novel strategy of using PHA granules for oriented enzyme immobilization.
- To explore the genetic designs, enzyme choices, and orientation control for this technique.
- To discuss current and potential applications of enzyme-immobilized PHA granules.
Main Methods:
- Genetic fusion of enzymes of interest to PHA synthase (PhaC).
- Intracellular production of functionalized PHA granules in bacterial hosts (e.g., E. coli).
- Isolation of functionalized PHA granules and assessment of their enzymatic activity.
Main Results:
- Functionalized PHA granules exhibit covalent attachment of active enzymes.
- This method achieves higher enzyme activity and product levels compared to non-oriented immobilization.
- Enzymatic activity is maintained under diverse assay conditions.
Conclusions:
- Enzyme immobilization via PHA synthase fusion is a promising technique for biocatalysis.
- It enables oriented enzyme presentation, enhancing catalytic efficiency.
- Potential applications span various industrial and research fields.
