Trehalose Stabilizes Lysozyme: A Biophysical and Docking Approach towards Understanding the Mechanism of Co-solute Engineering

Natural selection is believed to be an unforgiving and ceaseless force in the evolution of life on earth. An organism that cannot adopt a changing environment or an environmental hostile to cell functions is at risk as a species. So it is important to understand the mechanism used by the plants, animals and microorganisms in adapting to environments involve such stresses as extremes of temperature, pH, cellular hydration, desiccation, high extracellular salt environments and even the presence of denaturing concentration of urea inside cells. A phylogenetically diverse class of organisms can survive almost complete dehydration. Proteins in vitro lose their structure and function under such stress and, organism should die under such conditions, but organism survives due to presence of some wonder molecules through co-solute engineering by the nature. Included in this list are some plant seeds, fungal spores some nematodes, rotifers and cysts of some crustacean embryos such as the brine shrimp artemia. Nature has adopted a unique method to fight such stress. These organisms typically contain high concentration of many osmolytes that stabilize protein against different stresses and their presence does not alter protein activity. This study shows that trehalose provides the stability to the protein without bringing any change in the protein conformation. The Tm (midpoint of denaturation profile), an index of stability of protein, increases in the presence of trehalose. CD, fluorescence and UV-vis spectroscopy shows that structure of the protein remains intact in a wide range of trehalose. Molecular docking further validated these data.