Department of Chemistry, Jadavpur University, Kolkata-700 032, India E-mail: diptisingharoy@gmail.com, sbjuchem@yahoo.com Manuscript received 16 July 2018, accepted 24 August 2018 Fluorescence resonance energy transfer (FRET) from trypsin to a probe molecule, sodium salt of anthracene-1,5-disulfonate (1,5-AS) has specifically been used to monitor the extent of protein denaturation in buffer media. The data obtained from steady state fluorescence spectral studies and time resolved measurement indicated that the FRET from tryptophan (Trp) residue of trypsin to 1,5-AS occurred effectively in buffer medium. The stability of the complex formed between albumins and the probe has been recognized from the conformational changes of proteins. Steady state and time resolved studies in association with circular dichroism study have experimentally established the FRET efficiency and protein denaturation.