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Quaternary stabilization of a GH2 beta-galactosidase from the psychrophile A. ikkensis, a flexible and unstable dimeric enzyme
Protein Science 2025
Jan S. Nowak, Nikoline Kruuse, Helena Ø. Rasmussen, Pengfei Tian, Julie Astono, Søren Schultz-Nielsen, Mariane S. Thøgersen, Peter Stougaard, Jan Skov Pedersen, Daniel E. Otzen
Researchers investigated AiLac, a cold-active GH2 β-galactosidase from the psychrophilic bacterium Alkalilactibacillus ikkensis, to understand how its quaternary structure enables activity and stability at low temperatures. Flow Induced Dispersion Analysis (FIDA) was used, together with AlphaFold structure prediction and small-angle X-ray scattering, to support a reversible monomer–dimer equilibrium model for the enzyme. This quaternary flexibility, combined with a low dimer interface area, helped explain the enzyme's unusually low thermal and chemical stability as an extreme example of cold adaptation. It is an example of using FIDA to characterize protein oligomeric state and monomer–oligomer equilibria in solution.
