In this issue: Biotechnology Journal 1/2009

High‐throughput protein production Tegel et al., Biotechnol. J. 2009, 4, 51–57 Rapidly growing research in proteomics increases the need to produce recombinant proteins in a high‐throughput fashion. Researchers from Stockholm (Sweden) participate in an antibody‐based proteomics project to study protein expression and localization in human tissue and have optimized current protocols for recombinant protein production. The new procedure successfully reduces the number of handling steps and uses an automated protein purification system, both of which facilitate the handling of nearly 300 different proteins per week to optimize recombinant protein production. The procedure also allows to produce 600 recombinant proteins per month for antibody production. Furthermore, this protocol increases the efficiency of protein expression in E.coli cultures by 25%. Fully in vitro antibody screening Moutel et al., Biotechnol. Journal 2009, 4, 38–43 The phage display technique offers a rapid, inexpensive and animal‐free option to meet the increasing demand for antibodies in research and therapy, particularly in cancer therapy. However, a major obstacle for high throughput phage display is the production and purification of antigens as this is time consuming and needs to be adjusted for each antibody target. Researchers from the Institut Curie in Paris (France) present a new antibody selection approach by which antigens are produced through in vitro translation and can be used directly, without the need for purification. Using this new method, the authors successfully generate antibodies directed against GFP and the mammalian protein tsg101. Thus, this method is a promising tool to boost the antibody selection process in high‐throughput phage display. Biocatalyst performance van den Wittenboer et al., Biotechnology Journal 2009, 4, 44–50 The scope of technical biocatalysis is markedly extended by biphasic reaction media. But how can the various factors influencing catalyst performance be identified to ensure a successful implementation of catalytic processes? Lasse Greiner and coworkers from Aachen (Germany) propose a reactor setup by which biocatalyzed reactions in biphasic systems with distinct phases can be comprehensively characterized and optimized. The authors use small volumes which increase reproducibility and decrease the use of solvent and catalyst. Also, a constant interfacial area and independently stirred phases keep superimposing effects at bay. The authors successfully apply their design to the enantioselective reduction of ketones by bacterial alcohol dehydrogenases, suggesting that the new reactor design can enhance industrial enzyme production by increased enzyme productivity and stability.