The diffusion of reaction intermediates limits the efficiency of many industrial biocatalytic pathways. The UNSW iGEM team has designed the Assemblase self-assembling scaffold system as the solution to this problem.

The Assemblase scaffold specifically and covalently co-localises enzymes in a modular system. As a result, substrate can be channelled between enzymes at a much more efficient rate, thanks to the increased concentration of metabolic intermediates in the proximate surroundings of the enzymes.

Head over to our description page to find out how our system has been constructed.

Our Assemblase scaffold has a range of advantages that make it ideal for a variety of applications. This includes it being highly thermostable and chemically resistant permiting our scaffold to be used at high temperatures, allowing for increased kinetic energy in our system and therefore an increased rate of catalysis.

The chosen attachment system also affords our scaffold modularity. This is desirable as it means the scaffold can be easily adapted for use in a range of pathways important in industry, bioremediation, and pharmaceutical synthesis. 

Head over to our design page to find out how we chose the best components for our system.

Over the past few months we have been busy cloning DNA, expressing and purifying some really cool proteins, and attaching proteins together through self-assembly and with the Spy/Snoop Catcher/Tag system.

We also got to perform some really awesome enzyme assays and FRET experiments, alongside modelling our enzyme kinetics with some mathematical magic.

On top of this, we executed molecular dynamics analysis, and grew our very own plants on agar plates in the lab. We had a great year and would absolutely love to share it with you. So, have a look around, and explore all things UNSW iGEM!