Computational Study on Temperature Driven Structure-Function Relationship of Polysaccharide Producing Bacterial...

Area of Science:

• Biochemistry
• Enzymology
• Biotechnology

Background:

• Glycosyltransferases (GTs) are crucial enzymes in synthesizing bacterial exopolysaccharides (EPS).
• Bacterial EPSs are increasingly in demand across pharmaceutical, food, and industrial sectors.
• The industrial utility of EPSs is contingent upon their thermal stability and resistance to degradation.

Purpose of the Study:

• To investigate the structure-function relationship of GT enzymes from bacteria with varying growth temperatures (mesophile, thermophile, hyperthermophile).
• To assess the impact of temperature adaptation on GT structural properties and enzyme-substrate interactions.
• To identify optimal GTs for industrial-scale bacterial polysaccharide production.

Main Methods:

• In silico analysis of GT enzymes from mesophilic, thermophilic, and hyperthermophilic bacterial sources.
• Evaluation of structural integrity and plasticity across different temperature-adapted GTs.
• Computational assessment of GT-UDP-glucose binding affinity and hydrogen bond interactions.

Main Results:

• GT structural integrity significantly increases from mesophiles to thermophiles to hyperthermophiles.
• Structural plasticity of GTs is inversely correlated with growth temperature, favoring mesophiles.
• Thermophilic GTs exhibit superior binding affinity (-5.57 to -10.70 kcal/mol) with UDP-glucose, forming more hydrogen bonds (355) and involving stabilizing amino acids (Phe, Ala, Glu, Tyr, Ser).

Conclusions:

• Temperature adaptation profoundly influences GT structure and function.
• Thermophilic GTs possess enhanced stability and binding characteristics suitable for industrial applications.
• Thermophile-derived GTs are recommended for optimizing industrial bacterial polysaccharide production.