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Phytase expressed and anchored on the cell surface of  Pichia pastoris  avoids the expensive and time-consuming steps of protein purification and separation. Furthermore, yeast cells with anchored phytase can be used as a whole-cell biocatalyst. In this study, the phytase gene of  Citrobacter amalonaticus  was fused with the  Pichia pastoris  glycosylphosphatidylinositol (GPI)-anchored glycoprotein homologue  GCW61 . Phytase exposed on the cell surface exhibits a high activity of 6413.5 U/g, with an optimal temperature of 60°C. In contrast to secreted phytase, which has an optimal pH of 5.0, phytase presented on the cell surface is characterized by an optimal pH of 3.0. Moreover, our data demonstrate that phytase anchored on the cell surface exhibits higher pH stability than its secreted counterpart. Interestingly, our  in vitro  digestion experiments demonstrate that phytase attached to the cell surface is a more efficient enzyme than secreted phytase.

Citrobacter amalonaticus Phytase on the Cell Surface of Pichia pastoris Exhibits High pH Stability as a Promising Potential Feed Supplement