Folding and Stability of recombinant Azoreductase enzyme from Chromobacterium violaceum

Publication date: Available online 18 September 2019Source: Enzyme and Microbial TechnologyAuthor(s): Kamalesh Verma, Debanjan Kundu, Lal Mohan Kundu, Ashish Kumar Singh, Vikash Kumar DubeyAbstractAzoreductase from Chromobacterium violaceum was characterized biophysically using experimental and computational tools. The in-silico docking and cross-linking experiments using glutaraldehyde suggest dimeric nature of the enzyme. The enzyme structure was modelled and also studied using circular dichroism (CD) spectroscopy which suggests 40% α- helix, 30% β- sheet and 30% random coils. In the modelled structure of the azoreductase, the cofactor flavin mononucleotide (FMN) binding energy was -3.8 kJ/mol. The binding of FMN affects the azoreductase-cofactor complex stability. The stability-folding studies indicate that the cofactor, FMN is required for folding, stability and activity. Overall, the data provides interesting insight into stability and biophysical parameters of the azoreductase protein.

Source: Enzyme and Microbial Technology - September 19, 2019 Category: Biotechnology Source Type: research