Using Pichia pastoris to Display Lipase LipB52 on Cell Surface
Author Information
Author(s): Jiang Zhengbing, Gao Bei, Ren Ren, Tao Xingyi, Ma Yushu, Wei Dongzhi
Primary Institution: State Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology, East China University of Science and Technology, Shanghai, P. R. China
Hypothesis
The study investigates the effectiveness of displaying lipase LipB52 on the surface of Pichia pastoris compared to Saccharomyces cerevisiae.
Conclusion
LipB52 displayed on Pichia pastoris is more stable and suitable for use as a whole-cell biocatalyst than when displayed on Saccharomyces cerevisiae.
Supporting Evidence
- The lipase LipB52 displayed on Pichia pastoris showed hydrolysis activity of 94 U/g dry cell.
- The optimum temperature for the displayed lipases was found to be 40°C at pH 8.0.
- The lipase displayed on Pichia pastoris retained over 90% activity after incubation at 60°C for 2 hours.
Takeaway
Scientists found a way to put a special enzyme on the outside of yeast cells, making it work better for certain jobs than when it was on a different type of yeast.
Methodology
The lipase gene lipB52 was fused with the FLO gene and transformed into Pichia pastoris, where it was expressed and displayed on the cell surface.
Limitations
The study does not address potential long-term stability or performance in industrial applications.
Digital Object Identifier (DOI)
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