Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations

Abstract

Here, circular dichroism (CD) spectroscopy, fluorescence spectroscopy, UV-Vis spectroscopy, SDS-PAGE, substrate SDS-PAGE, and molecular dynamics (MD) simulations techniques have been employed to understand the structural behavioral changes of trypsin (MW: 19.72 kDa, source: digestive system of adult Indian major carp, Catla C. catla) in the presence of various chemical environments. The stability of the trypsin can be increased by stabilizers, including trimethylamine N-oxide (TMAO), proline, and betaine, without affecting its native structure. Trypsin has shown unusual high thermal stability in the presence of betaine. Further, these experimental results were confirmed by means of MD simulations. The present results explicitly elucidated that the behavior of a co-solvent may vary depending upon the type of the protein.