The extracellular medium-chain-length (mcl) PHA depolymerase (ePhaZMCL) is able to degrade extracted, denatured mcl-PHA. It contains a putative substrate-binding domain (SBD) and a catalytic domain. In our Laboratory, we established a high yield expression system for a recombinant, active and secreted ePhaZMCL and for an inactive and secreted ePhaZMCL containing only the SBD (ePhaZMCL-SBD). Both ePhaZMCL and ePhaZMCL-SBD can be used for targeted immobilization of proteins onto mcl-PHA surface through SBD. To this purpose, we fabricated micro/nano-scaled mcl-PHA beads. In contrast to standard methods for emulsion-based polymer bead production, detergents are not needed in our process. The mcl-PHA beads can be used for non-specific as well as targeted immobilization of proteins. The binding capacity is comparable to similar-sized polystyrene particles used e.g. for antibody immobilization in latex agglutination tests. Similar applications can be envisaged for mcl-PHA latex given a high capacity for antibody adsorption observed in our studies. The ePhaZMCL-SBD and mcl-PHA system may be used for drug delivery to specific target cells in the human body. The advantages of mcl-PHA carriers would be the avoidance of detergents and a high degree of biocompatibility combined with degradation via (slow) surface erosion. The ePhaZMCL may also have other biocatalytic applications.
Contact:
Dr. Qun Ren
Qun.Ren@empa.ch
Tel.: +41 (0)58 765 76 88 |
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