Peter Westh, Kim Borch, Trine Sørensen, Radina Tokin, Jeppe Kari, Silke Badino, Mafalda A Cavaleiro, Nanna Røjel, Stefan Christensen, Cynthia S Vesterager, Corinna Schiano-di-Cola
We have measured activity and substrate affinity of the thermostable cellobiohydrolase, Cel7A, from Rasamsonia emersonii over a broad range of temperatures. For the wild type enzyme, which does not have a Carbohydrate Binding Module (CBM), higher temperature only led to moderately increased activity against cellulose, and we ascribed this to a pronounced, temperature induced desorption of enzyme from the substrate surface. We also tested a "high affinity" variant of R. emersonii Cel7A with a linker and CBM from a related enzyme...
April 2018: Biotechnology and Bioengineering