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Related Experiment Video

Updated: Jun 16, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

[Sortase analysis by displaying its substrates on yeast surface].

Lixin Luo1, Lin Wu, Ying Lin

  • 1College of Veterinary Medicine, National Reference Laboratory of Veterinary Drug Residues, Guangdong Provincial Key Laboratory of Veterinary Pharmaceutics Development and Safety Evaluation, South China Agricultural University, Guangzhou 510642, China. btlxluo@scut.edu.cn

Wei Sheng Wu Xue Bao = Acta Microbiologica Sinica
|February 2, 2010
PubMed
Summary
This summary is machine-generated.

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Sortase substrates were successfully displayed on Pichia pastoris yeast cells using enhanced green fluorescent protein (EGFP) for detection. This method enables a reliable assay for sortase activity in yeast.

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Microbiology

Context:

  • Cell surface display is a powerful technique for protein expression and functional analysis.
  • Pichia pastoris is a widely used yeast host for recombinant protein production due to its robust secretory pathway and post-translational modification capabilities.
  • Sortases are enzymes that catalyze the covalent attachment of proteins to cell surfaces, offering a method for protein immobilization.

Purpose:

  • To develop a method for displaying sortase substrates on the surface of Pichia pastoris.
  • To utilize enhanced green fluorescent protein (EGFP) as a reporter for successful surface display and sortase activity.
  • To establish a novel assay for quantifying sortase activity in a yeast expression system.

Summary:

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Last Updated: Jun 16, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
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Protein Engineering by Yeast Surface Display
05:49

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Published on: November 29, 2024

Microarray Analysis for Saccharomyces cerevisiae
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  • The gene encoding a QALPETGEE sortase substrate fused to EGFP was constructed and introduced into Pichia pastoris.
  • Recombinant yeast cells expressing the fusion protein were confirmed via fluorescence microscopy.
  • Sortase activity was quantified by measuring the fluorescence intensity of released EGFP using a fluorescence spectrophotometer, showing a significant increase after enzymatic activity.

    • Impact:

    • This study demonstrates the successful display of functional sortase substrates on yeast cell surfaces.
    • The developed system provides a novel and efficient platform for sortase activity assays.
    • This approach has potential applications in protein engineering, biocatalysis, and diagnostics.