The Surface Display of Lipase on a Pastoris pichia and Analysis of Fermention Process
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Abstract:
In this research, the activities of enzyme displaying on the surface of pastoris pichia and enzyme in the fermentation supernatant of two recombinant displaying yeast were studied, which were based on two surface yeast display systems with the flocculation functional domain of FLO1p and α-agglutinin functional domain respectively. In the process of displaying the lipase on the yeast cell surface, some secreted lipases were found in supernatants. With the identification of active lipase, the glycosylation assay and the mounts increase of foreign protein, the reason that interest lipase were secreted into the supernatant to the great extent was resulted from unstable non-covalence bond between the flocculation functional domain of Flo1p and mannose in the cell wall. The study provided theoretical guide for efficient display of lipase on a pastoris pichia and improve the catalytic activity of displaying enzymes.
