The aggregation of a recombinant lipase as inclusion bodies (IBs) was studied directly within intact Escherichia coli cells by FT-IR microspectroscopy. Through this approach, it was possible to monitor in real time the different kinetics of IB formation at 37 and 27 degrees C, in excellent agreement with the results of the SDS-PAGE analysis. Furthermore, insights on the residual native-like structure of the expressed protein within IB--both isolated and inside cells--were obtained by the secondary structure analysis of the Amide I band in the IB FT-IR spectra.
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Ami et al. (2005) studied this question.