Researchers from Michigan State University (MSU), the US, have found an efficient way to improve the yield of biopharmaceutical production by freeing up protein trapped in bacterial stores known as inclusion bodies. Inclusion bodies are insoluble aggregates that are formed by bacteria to store excess recombinant protein produced during expression. These are hard to separate during bioprocessing and indicate that up to 95 per cent of the protein expressed by the bacterial culture is not usable.
A team of scientists, led by chemist David Weliky of MSU, identified a way of delving into the secondary structure of these inclusion bodies using nuclear magnetic resonance spectroscopy. This, according to Weliky, means that it may be possible to extract the protein from the inclusion bodies without separating and refolding.
With the world protein therapeutics market expected to grow from $ 63 billion in 2007 to $ 87 billion in 2010, there is a pressing need to boost manufacturing capacity and streamline the production of proteins. "This approach will be applicable to the structural analysis of many inclusion body proteins and should provide useful information for optimising solubilisation and purification protocols of these proteins," said the researchers.
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