Although aerobic CO dehydrogenases (CODHs) might be applicable in various fields， their practical applications have been hampered by low activity and no heterologous expression. We， for the first time， could functionally express recombinant PsCODH in E. coli and obtained a highly concentrated recombinant enzyme using an easy and convenient method. Its electron acceptor spectra， optimum conditions (pH 6.5 and 30 °C)， and kinetic parameters (k of 12.97 s， K of 0.065 mM， and specific activity of 0.86 Umg) were examined. Blast furnace gas (BFG) containing 20% CO， which is a waste gas from the steel-making process， was tested as a substrate for PsCODH. Even with BFG， the recombinant PsCODH retained 88.2% and 108.4% activity compared with those of pure CO and 20% CO， respectively. The results provide not only a promising strategy to utilize CO-containing industrial waste gases as cheap， abundant， and renewable resources but also significant information for further studies about cascade reactions producing value-added chemicals via CO as an intermediate produced by a CODH-based CO-utilization system， which would ultimately expand the versatility of CODH.