Sekisui Diagnostics sponsored research at the University of Oxford announces remarkable results
The UK R&D group of Sekisui Diagnostics are proud to announce that a research project in the Biochemistry Department at the University of Oxford, UK, sponsored by Sekisui Diagnostics, has published its first scientific paper which is featured on the Biotechnology and Biosciences Research Council (BBSRC) web site.
In this project a PhD student at Oxford, Chris Schoene, is using a new technique to make enzymes retain their activity, even after boiling. This technique adds extra elements called ‘SpyTag’ and ‘SpyCatcher’, which have been designed to attach to each other, into an enzyme molecule. Each enzyme molecule is naturally made with a long chain structure, folded around on itself in various ways to create the biochemical activity of the enzyme. Harsh conditions such as heating will disrupt this chain structure and kill the activity of the enzyme. Chris Schoene has shown that SpyTag and SpyCatcher can be added to each end of the chain in the enzymes Beta-Lactamase and Dihydrofolate Reductase and allow them to retain their activity to a remarkable extent, even after boiling.
The Beta-Lactamase used in this work was chosen as a model system because it has quite a simple molecule structure and it is easy to measure its activity. It is not the same enzyme as those currently manufactured and sold by Sekisui Diagnostics as it does not have the right range of activity to be useful to our customers. However, the Oxford project now aims to discover whether this SpyTag/SpyCatcher technology can also be used with more commercially important enzymes.
The Sekisui R&D scientists involved in supporting this project are Paul Bennett, Lee Bezuidenhout, Ernest Asilonu, Xingmin Li and Nick Major. Paul has made a significant scientific contribution to the work and he is named as a co-author of the recently-published scientific paper.
This project demonstrates that Sekisui Diagnostics is investing to push forward the boundaries of biochemical knowledge and investigate new ways to improve the properties of enzymes. We are delighted to have been chosen as partners by one of the world’s leading Biochemistry research universities and the major funding party for the project, the UK’s Biotechnology and Biosciences Research Council (BBSRC). We look forward to more exciting advances in the course of this project.