Article ID Journal Published Year Pages File Type
2052697 FEBS Letters 2005 4 Pages PDF
Abstract

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 °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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