Pilot-scale production of recombinant LeIBP from Arctic yeast Glaciozyma sp. by Escherichia coli

Abstract

Antifreeze proteins (AFPs) have a unique feature to bind to ice nuclei, and are referred to ice-binding protein (IBP). The AFP, expressed in the cells of some polar organisms, controls cell damage in subzero temperature environments by inhibiting the ice growth and recrystallization. In this study, recombinant LeIBP (Leucosporidium ice-binding protein) from the arctic yeast Glaciozyma sp. (former known as Leucosporidium sp.) was produced in E. coli using a cold shock induction system. The final cell density and concentration of the purified LeIBP were measured to be 8.2 g/L and 1.1 g/L, respectively. The thermal hysteresis (TH) activity of LeIBP was 0.39 ± 0.02°C at 13.25 mg/ml, which means that the scale-up was successfully performed for the production of recombinant LeIBP in heterologous bacterial expression system.