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- W2029272253 abstract "A novel surface-display system was constructed using the cell-wall anchor protein Flo I p from Saccharomyces cerevisiae, the mannanase (man I from Bacillus subtilis fused with the C-terminus of Flo I p and the 6 x His tag was inserted between Flo l p and man I. The fusion protein was displayed on the cell surface of Yarrowia lipolytica successfully, and it was confirmed by immunofluorescence. In succession, the surface-displayed mannanase was characterized. The optimum catalytic conditions for the recombinant mannanase were 55 °C at pH 6.0, and it exhibited high stability against pH variation. The highest activity of the recombinant mannanase reached 62.3 IU/g (dry cell weight) after the recombinant was cultivated for 96 h in YPD medium [I % (w/v) yeast extract/2 % (w/v) peptone/2 % (w/v) glucose]. To our knowledge, the present paper is the first to report that high-activity mannanase is displayed on the cell surface of Y. lipolytica with Flo I p." @default.
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- W2029272253 date "2009-10-13" @default.
- W2029272253 modified "2023-09-25" @default.
- W2029272253 title "Cell-surface display of the active mannanase inYarrowia lipolyticawith a novel surface-display system" @default.
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- W2029272253 doi "https://doi.org/10.1042/ba20090222" @default.
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