The protein folding/unfolding process represents today in science a deep open question. We thus decided to investigate the unfolding process of beta-lactoglobulin (LG) which involves different steps and did already preliminary studies under high pressure. Within the framework of the long term proposal LTP 8-4 (see ILL report LTP 8-4) we probed the protein on D16 and IN16 under high pressure and got interesting results with respect to the large scale structure and dynamics. Some of the involved processes take a rather long time to be fully achieved (several hours or days). This emerged through changes over time during measurements at a specific pressure and temperature. Indeed several competitive effects may participate to the unfolding mechanism as aggregation, partial unfolding and water insertion. We thus wish to further investigate the system to better understand the consecutive steps and their meaning.