As most of the proteins are going into the insoluble fraction as an aggregate and a very low amount in soluble fraction...
I recommend reading one of the many excellent review articles that describe the different strategies as you and may need to try more than one. In my experience lowering the overall expression of the protein usually increases soluble yield. You can lower expression in many ways, minimal (or less rich) media, lower expression temperature, shorter expression time, different promotor.....
Inclusion body separation protocol
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518028/
Dear Santhosh
I think with Jeffrey suggestion you can find a way to purify the inclusion bodies. Some authors think that expression in inclusion bodies is an advantage due to low hydrolisis rate and protection to toxic effect, I think is a collateral effect than you can take benefit. In my experience the fast refolding methods produce better results (less agregation) than usually low dilution rate ones (dialysis or solvent exchange), but it will depend on how hydrophobic is your protein as Jörg said.
http://link.springer.com/article/10.1007%2Fs12033-012-9573-0
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