My recombinant protein, cellulase, produced in E.coli. I remove small domain from it. I think when my protein produce in high concentration, its activity is reduced.
While proteins are prone to aggregation at higher concentrations the point of such aggregation can vary tremendously from protein to protein. I have worked with proteins that had formed aggregates at 10uM concentrations and proteins that were stable at 1-2mM concentrations. Chicken egg white albumin can reach 100mg/ml without aggregation.
In your particular case I would suggest to confirm the presence of aggregates by measuring the light scattering as function of protein concentration, this could be done in visible spectrum at 600nm.
At infinite dilution, there is no aggregation. So there is a necessary relationship between concentration and aggregation.
Aggregation always is a reaction of 2nd or higher order. This means by definition that it is dependent on protein concentration. The more likely it is for two particles to find each other in a solution the more likely it is that they interact/aggregate.
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