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Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
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Engineering and application of enzymes for lipid modification, an update
Katja Zorn1, Isabel Oroz-Guinea1, Henrike Brundiek2
1Institute of Biochemistry, Dept. of Biotechnology & Enzyme Catalysis, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany.
Progress in Lipid Research
|June 16, 2016
Summary
Protein engineering tools like directed evolution and rational design optimize enzymes for biocatalysis. This review highlights engineered enzymes, including lipases and others, for improved industrial applications.
Area of Science:
- Biochemistry and Molecular Biology
- Enzyme Engineering
- Biocatalysis
Background:
- Protein engineering is crucial for tailoring enzyme properties for specific applications.
- Directed evolution and rational design are key strategies for enzyme optimization.
- High-throughput screening accelerates the identification of improved enzyme variants.
Purpose of the Study:
- To review essential protein engineering tools and strategies.
- To showcase literature examples of enzyme optimization for biocatalysis.
- To discuss recent advancements in engineered enzymes for industrial use.
Main Methods:
- Introduction to directed evolution and rational protein design.
- Integration of high-throughput screening methodologies.
- Literature survey of enzyme optimization case studies.
Main Results:
- Engineered lipases demonstrate altered fatty acid selectivity and enhanced esterification.
- Optimized phospholipases, lipoxygenases, and P450 monooxygenases are discussed.
- Progress in engineered decarboxylating enzymes, fatty acid hydratases, and cascade reactions is presented.
Conclusions:
- Protein engineering significantly enhances enzyme performance for biocatalytic processes.
- Diverse enzyme classes, including lipases, have been successfully engineered.
- Future applications of engineered enzymes in industrial chemistry are promising.
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