Large scale therapeutic protein production is not so cheap, and it is well known that pharmaceutical industry is under constant pressure to reduce the overall costs. When post-translational modification requirements allow to adopt in production yeast systems instead of mammalian cells, the cost is significantly lowered. In this latter case, the selection of high-producing clones is very important and the possibility to visually discriminate just in 3-4 classes the productivity of thousands of clones in a few days by a single operator is noteworthy, especially if the method is cheaper than classic ELISA or fluorescence/bioluminescence test.
So Hribar and colleagues from the National Institute of Chemistry of Ljubljana, started to deal with alternative “low cost” reporter genes like the beta-lactamase, to find out a rough measure of the protein of interest. The autors worked on Pichia pastoris, a yeast strain just licensed to more than 100 companies also for recombinant heterologous protein production. The short technical report published on the april number of Biotechniques, will not warm up any reporter geek - like me - that loves stupid performances (who really need 9 orders of magnitude linearity???), but the colorimetric method of such 39 kD b-lactamase enzyme would be an asset for smart bio-companies which prefer pragmaticity to geekiness.---/ citation /--- --- ---
Hribar, G., Smilović, V., Lenassi Zupan, A., & Gaberc-Porekar, V. (2008). β-lactamase reporter system for selecting high-producing yeast clones BioTechniques, 44 (4), 477-484 DOI: 10.2144/000112730