DMSO strengthens chitin deacetylase-chitin interaction: Physicochemical, kinetic, structural and catalytic insights

•Chitin deacetylase enzyme from P. laurentii purified and characterized.•Relative enzymatic activity enhanced in the presence of DMSO.•DMSO had no effect on secondary structure of the enzyme.•DMSO caused tertiary structural changes in the enzyme.•Stronger enzyme-substrate interaction involving residues in the catalytic domain. Chitin deacetylase, an enzyme isolated from Cryptococcus laurentii RY1, catalyzes the hydrolysis of acetamido group of N-acetyl-D-glucosamine unit of chitin. The primary objective of this study was to characterize and comprehend the activation of chitin deacetylase by DMSO. The secondary structure of the protein was determined by circular dichroism(CD).The interaction of protein with DMSO was evaluated by CD and tryptophan fluorescence spectroscopy which revealed that DMSO had no effect on overall secondary structure, but induced change in the tertiary structure of the enzyme. The interaction of chitin deacetylase with chitin in DMSO system when investigated by molecular dynamics simulation revealed stronger chitin deacetylase-chitin interaction involving several amino acid residues. The enhanced activity of the enzyme in presence of DMSO along with the fact that its kcat is highest of all other reported chitin deacetylases makes it a superior candidate in the industrial sector involved in chitosan production from chitin.