You wish to produce a human enzyme, protein A, by introducing its gene into bacteria.The genetically engineered bacteria make large amounts of protein A, but it is in the
form of an insoluble aggregate with no enzymatic activity. Which of the following procedures might help you to obtain soluble, enzymatically active protein? (Hint: Some
proteins require molecular chaperones in order to fold properly within the environment of the
cell. )
(a) Treat the insoluble aggregate with a protease.
(b) Make the bacteria overproduce chaperone proteins in addition to protein A.
(c) Heat the protein aggregate to denature all proteins, then cool the mixture.
(d) None of the above.
I'm leaning towards (a) as my answer, but I'm not too sure.
To obtain soluble, enzymatically active protein A, one possible approach is to make the bacteria overproduce chaperone proteins in addition to protein A. Chaperone proteins are known to assist in the correct folding of newly synthesized proteins, preventing them from forming insoluble aggregates.
Option (a) to treat the insoluble aggregate with a protease may not be effective because using a protease would likely degrade the proteins, including protein A, rather than promoting proper folding.
Similarly, option (c) to heat the protein aggregate to denature all proteins and then cool the mixture may not be the best approach since it could disrupt the structure of protein A and potentially render it inactive.
Therefore, the most suitable option in this case is (b) - making the bacteria overproduce chaperone proteins in addition to protein A. This mechanism of increased chaperone production can enhance the chances of proper folding and solubility of protein A, resulting in its enzymatic activity.