Performance of beta-galactosidase inclusion bodies in enzymatic bioprocesses
© García-Fruitós et al; licensee BioMed Central Ltd. 2006
Published: 10 October 2006
Inclusion body formation is a common event during bacterial over-expression of recombinant genes. This phenomenon represents a great matter of concern in biotechnology, because it has restricted the spectrum of proteins marketed in this field. In a previous work, we have observed that recombinant enzymes produced in bacteria are not completely inactivated when deposited as inclusion bodies  and that aggregation as inclusion bodies does not necessarily split protein population into active and inactive fractions. Therefore, we decided to further explore and fully characterize the behaviour of purified beta-galactosidase inclusion bodies in presence of substrate, during a small-scale bioprocess.
We could conclude that, interestingly, when an enzyme aggregated as inclusion bodies is incubated with its substrate, part of this protein might be spontaneously solubilised in a process that seems to be eventually favoured by the presence of substrate. Moreover, this soluble protein shows considerable enzymatic activity that is a major contributor to the enzymatic process initiated by inclusion bodies.
This work has been funded by BIO2004-00700 from MEC, Spain and 2005SGR-00956 (AGAUR). Elena García-Fruitós is recipient of a doctoral fellowship from MEC, Spain.
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