Effect of osmolytes on the enzymatic properties of bovine chymotrypsin

Osmolytes are small solutes that regulate turgor pressure within cells that undergo various extreme stressors from high salt or urea concentration, drastic pressures, high temperatures, among other parameters. Since their mechanism of action is not well understood, the emphasis in most scientific investigations is to study their effect on the structure, function, and stability of proteins and enzymes. In my research work described in this presentation I have studied the effect of different concentrations of osmolytes such as urea, guanidine hydrochloride, betaine, trimethylamine-N-oxide (TMAO) on the enzymatic properties of a serine protease, bovine chymotrypsin. Serine proteases are proteolytic enzymes that have crucial role in bodily functions by performing specific peptide bond hydrolyses in proteins and peptides. Bovine chymotrypsin shows specificity towards large hydrophobic amino acid side chains such as Leu, Phe, Tyr, and Trp but also hydrolyzes peptide bonds contributed by Arg. In my research investigations I used substrates bearing Leu, Phe, and Arg at the reactive site peptide bond. The results of this investigation will be presented in terms of effects of osmolytes on the enzymatic hydrolysis of different substrates by bovine chymotrypsin