Well, the solution is a better description of your protein. P.e is it globular .... or have you found the kind of it in references.
What a kind of buffer and what a pH are you using?
On other part, the solubility of a protein depends of several factors like temperature, pH-value, dieletric constante of the solvent + buffer and you must know the I.P. of your protein.
pH -values above or under the I.P. govern the solubility or aggregation.
What a kind of spectrometer and cuvettes are you using?
Please note that answerers need always more infos for a good answer e.g. solution.
You may try adding polyols such as sorbitol. High concentrations of sorbitol can stabilize proteins by raining their thermal denaturation temperature. We have successfully used sorbitol to stabilize B-Lactoglobulin against unfolding at >75°C. IN this work we used CD spectroscopy to determine stability. For more details you may wish to refer to the paper below and references therein.
Modulating β-Lactoglobulin Nanofibril Self-Assembly at pH 2 Using Glycerol and Sorbitol
The isoelectic point of the protein is 7.8, and we are using a buffur (sod. phosphate buffer) of pH 8., the protein is globular in nature and since it has concenteration dependent aggregation, therefore, concentration has been kept low, for measurement of CD spectra at high temp, we need to incubate the protein for certain time, here we found aggregation, additives most often produces noise and gives strong signal in the far UV range. I need information on the solubility of this protein at elevated temperature. What colud be added that doesn't interfares with CD and fluorascence signals.
Thanks for the additional information Rakesh, Indeed, the additives like glycerol and sorbitol had high absorption in our study too. In my experience, the noise levels can be reduced by using a slightly more concentrated sample and reducing the pathlength of the cuvette.