Development of a microtiter plate-based assay for the detection of lipase-catalyzed transesterifications in organic solvents
Related Experiment Video
Updated: Apr 21, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Martin Pöhnlein1, Tim Finkbeiner, Christoph Syldatk
1Institute of Process Engineering in Life Sciences, Section II: Technical Biology, Karlsruhe Institute of Technology (KIT), Engler-Bunte-Ring 1, 76131, Karlsruhe, Germany, martin.poehnlein@kit.edu.
Abstract:
A microtiter plate-based assay was developed to evaluate the ability of lipases to perform transesterifications when employed in different organic solvents. A 4-nitrophenol assay was carried out employing seven different lipase formulations and two fatty acid methyl esters with different chain lengths in a total of six organic solvents with logP values approximately between 1 and -1. This assay delivered results within comparatively short times measured by a color reaction and thus facilitates the choice of an enzyme-solvent combination for the synthesis of glycolipids. To validate the findings, glycolipid syntheses were performed using the same lipase formulation in the same solvents. When comparing the results obtained using the microtiter plate-based assay to the results of the glycolipid syntheses using the same lipases and solvents, matching results were obtained.
More Related Videos
07:37Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening
Published on: May 13, 2020
13:02Arabidopsis thaliana Polar Glycerolipid Profiling by Thin Layer Chromatography TLC Coupled with Gas-Liquid Chromatography GLC
Published on: March 18, 2011