I would be cautious. The lore around protein expression in E. coli is that fresh cultures will always be better, but if the cells easy express your protein and it folds w/o too much trouble, you may be OK. It's protein-dependent. If you have an assay, perhaps your protein is an enzyme, or if it binds to something that is readily quantified, that's the real check.

I assume this is done in TB media and the 1.0 OD was induction done at mid-log phase?  What is the goal for this production and is the expression soluble or insoluble?  It might be better to start over again since the stress response to these environmental shifts may impact not only the protein integrity but also the contaminants.  But you continued the culture for a reason; perhaps because the final use of the protein, the timeline, or the time, or production scale investment determined that the risks would be worth it if  adverse results would be minimal or of no major consequence?  Since you already have the culture going, I hope the expression is insoluble because that may be the lowest risk scenario. A gel and LC/MS may be needed and if it's a soluble expression then hopefully there's an affinity tag to help quickly pull out a small sample for the same kind of analysis.  By now the culture has been harvested/frozen and maybe you can make a decision to process further (folding, purification, etc.) from the current commentary.

Thank you all for the answers. Yes Grant you guessed correctly; I do have a very tight time constraint which is why I decided to proceed with this culture. The OD is increasing, slowly, but its on its way to the optimum. Will see if this yields the protein I want or not. 

Ok everyone for future reference: This batch was a fail.