Structural Studies of the Cellulase Enzyme (CEL7465) from Fimbriimonadales Using Small-Angle X-ray Scattering

The effectiveness of biotechnological processes depends on the stability of the enzymes used in them, including their temperature stability, stability in high salt concentrations, and stability at extreme pH values. This is especially important for enzymes used in the food, paper, textile, and chemical industries, such as pectinases, cellulases, and alpha-amylases. The most sought-after enzyme in many biotechnological processes is cellulase, which has led to its widespread use and rapid spread on the global market. The structural features of a new thermostable cellulase, Cel7465, isolated from a thermal spring in the Republic of North Ossetia-Alania were investigated. Through comparative analysis of the cel7465 gene sequence against known nucleotide sequence databases, we were able to assign this gene to a non-cultivable microorganism belonging to the Fimbriimonadales order. The system of expression and purification of recombinant Cel7465 protein was optimized. The small-angle X-ray scattering method was used to investigate the structural features of the enzyme.