Expression of the sucrose binding protein from soybean: Renaturation and stability of the recombinant protein

A sucrose binding protein from soybean, which contains two conserved barrel domains (1) of the cupin superfamily, was bacterially produced, affinity-purified, renatured and characterized. The refolded his-tagged protein regained its sucrose binding capacity and it was highly thermo and chemical stable, suggesting it was properly folded into a bicupin structure.