An Oxford DPhil student has discovered that treating enzymes with a bacterial superglue allows them to be boiled without loss of function.
Being able to stabilize enzymes in this way could have huge benefits for manufacturing processes and products that use enzymes – naturally occurring molecules with a wide variety of functions. It could improve biofuel production, diagnostics products, and food industry processes.
Chris Schoene, a PhD candidate mid-way through a BBSRC CASE studentship at the University of Oxford, used the bacterial ‘glue’ called SpyTag to stick opposite ends of enzymes together and form a closed loop.
This had a dramatic effect on the resilience of one enzyme, β-lactamase, allowing it to be boiled and still retain a high level of function. Chris then tested the method on another enzyme, Dihydrofolate reductase, and found it too was able to retain function after boiling.
Isis Innovation, the University of Oxford’s technology transfer company, has been working with Professor Mark Howarth, whose team created the SpyTag superglue, to protect the intellectual property and work with commercial partners to take the project further.
Professor Howarth said: “Most of our work on SpyTag has been on using it to link different things together, such as for tracking receptors on cells or binding proteins to magnetic beads for sensitive capture of rare cells in blood. Chris’ discovery of this new route to resilient enzymes has opened up a whole new direction for us to explore.”
The team believes that locking the enzyme with SpyTag did not prevent the enzyme from altering shape when heated, but rather allowed it to return to the correct formation when cooled back down. Only in the correct formation is an enzyme able to maintain its function.
The team now plans to apply this technology to other industrially important enzymes in collaboration with Sekisui Diagnostics.
