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Related Experiment Video

Updated: May 4, 2026

Quantitative Analysis of the Cellular Lipidome of Saccharomyces Cerevisiae Using Liquid Chromatography Coupled with Tandem Mass Spectrometry

Quantitative Analysis of the Cellular Lipidome of Saccharomyces Cerevisiae Using Liquid Chromatography Coupled with Tandem Mass Spectrometry

Published on: March 8, 2020

Quantification analysis of yeast-displayed lipase.

Zi Jin¹, Kun Zhang¹, Li Zhang¹

¹Guangdong Key Laboratory of Fermentation and Enzyme Engineering, School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, PR China.

Analytical Biochemistry

|January 11, 2014

Summary

A new method quantifies displayed lipase on yeast cell surfaces using a fluorescent tag. This reliable technique accurately measures lipase levels, aiding surface display research.

Keywords:

Active-site titration Lipase Quantification Yeast surface display

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Last Updated: May 4, 2026

Quantitative Analysis of the Cellular Lipidome of Saccharomyces Cerevisiae Using Liquid Chromatography Coupled with Tandem Mass Spectrometry

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Published on: March 8, 2020

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Published on: August 21, 2009

Analysis of Lipid Droplet Content in Fission and Budding Yeasts using Automated Image Processing

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Published on: July 17, 2019

Area of Science:

Biotechnology
Enzymology
Molecular Biology

Background:

Yeast surface display is a powerful system for protein engineering and enzyme evolution.
Accurate quantification of displayed proteins, like lipase, is crucial for optimizing yeast display systems.
Existing methods for lipase quantification may have limitations in sensitivity or applicability.

Purpose of the Study:

To develop and validate a novel method for quantifying cell surface-displayed lipase on yeast.
To establish a reliable and sensitive assay for measuring lipase expression levels in yeast surface display systems.
To provide a tool that facilitates advancements in lipase engineering and applications.

Main Methods:

Utilized an organophosphonate ester to irreversibly inhibit active lipase.
The inhibition reaction released a detectable fluorescent group, proportional to lipase activity.
Quantified displayed lipase in terms of mass per cell mass (g/g cell) and molecules per cell.

Main Results:

The developed method demonstrated accurate quantification of displayed lipase.
Results from this method showed strong correlation with established quantification techniques.
The assay proved to be a credible and sensitive tool for lipase measurement.

Conclusions:

The described method offers a credible and powerful approach for quantifying yeast-displayed lipase.
This technique will significantly support and advance research in lipase surface display technology.
The fluorescent-based assay provides a valuable tool for enzyme engineering and bioprocess development.