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Published on: April 22, 2016
Enhanced ethyl butyrate production using immobilized lipase
Selma Ateş1, Burcu Türk, Emine Bayraktar
1Gazi University, Faculty of Science, Chemistry Department , Ankara , Turkey.
Artificial Cells, Nanomedicine, and Biotechnology
|January 12, 2013
Summary
This study optimized ethyl butyrate production using immobilized lipase. Response surface methodology identified ideal conditions, achieving 61.3% conversion, which increased to 90.3% with Na2HPO4.
Area of Science:
- Biocatalysis
- Enzyme Immobilization
- Ester Synthesis
Background:
- Ethyl butyrate is a valuable ester with applications in flavors and fragrances.
- Lipase-catalyzed esterification is a common method for ethyl butyrate production.
- Enzyme immobilization enhances lipase stability and reusability.
Purpose of the Study:
- To optimize the production of ethyl butyrate using immobilized lipase.
- To determine the optimal reaction conditions for maximum ester conversion.
- To evaluate the effect of Na2HPO4 on the esterification process.
Main Methods:
- Enzyme immobilization of lipase.
- Shake flask experiments for ethyl butyrate synthesis.
- Response surface methodology (RSM) for optimization of reaction parameters.
- Gas chromatography (GC) for analyzing product conversion.
Main Results:
- The optimized conditions yielded a maximum initial conversion of 9.1%.
- Optimal conditions included 0.31 M substrate concentration, an acid-alcohol molar ratio of 0.49, 25% (w/v) immobilized enzyme at 35°C for 3 hours.
- A conversion of 61.3% was achieved after 55 hours under optimized conditions.
- The addition of Na2HPO4 to the reaction medium significantly increased the conversion to 90.3% within 55 hours.
Conclusions:
- Response surface methodology is effective for optimizing ethyl butyrate production.
- Immobilized lipase offers a viable biocatalyst for efficient ester synthesis.
- Na2HPO4 significantly enhances the lipase-catalyzed production of ethyl butyrate, achieving high yields.
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