Optimizing lipases and related enzymes for efficient application
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Updated: Sep 29, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Uwe T Bornscheuer1, Cornelius Bessler, Ramisetti Srinivas
1Institute of Chemistry & Biochemistry, Department of Technical Chemistry & Biotechnology, Greifswald University, Soldmannstr. 16, D-17487 Greifswald, Germany. uwe.bornscheuer@uni-griefswald.de
Abstract:
Although numerous reactions have been performed using lipases and related enzymes (e.g. esterases and phospholipases), it is still a challenge to identify the most suitable biocatalyst and best reaction conditions for an efficient application. Frequently used methods such as immobilization and optimization of the reaction medium cannot be transferred from one reaction system or substrate to another. However, in the past few years, rational protein design and directed evolution have emerged as efficient alternative methods to optimize biocatalytic reactions.
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