Cloning, expression, and purification of the N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae in Pichia pastoris

► A more efficient way to purify N-Flo1p from Saccharomyces cerevisiae was obtained by producing it in Pichia pastoris. ► The yield obtained with this organism is more than 4 times higher compared to S. cerevisiae as an expression organism. ► The protein was produced with a significant improvement in homogeneity of its glycosylation state. ► The binding activities of N-Flo1p produced by P. pastoris and S. cerevisiae are similar.