An efficient system for catalyzing ester synthesis using a lipase from a newly isolatedBurkholderia cepaciastrain

Autor:	Erika Zago, Thais Fabiana Chan Salum, J. Baratti, V. Turra, Nadia Krieger, David A. Mitchell, Alessandra Machado Baron
Rok vydání:	2008
Předmět:	chemistry.chemical_classification biology Immobilized enzyme Triacylglycerol lipase biology.organism_classification Biochemistry Micelle Catalysis Burkholderia Enzyme chemistry Biocatalysis biology.protein Organic chemistry Lipase Bacteria Biotechnology
Zdroj:	Biocatalysis and Biotransformation. 26:197-203
ISSN:	1029-2446 1024-2422
DOI:	10.1080/10242420701568674
Popis:	The synthesis of ethyl-oleate by the lipase from the newly isolated strain Burkholderia cepacia LTEB11 in three different systems has been studied – immobilization on a hydrophobic support (Accurel EP 100®), encapsulation in reverse micelles, and direct addition of powdered free enzyme to the reaction medium. The immobilized enzyme performed best, giving a 70% ester yield in 10 h, this yield being five-fold greater than that obtained for reversed micelles, and two and a half times greater than that obtained for direct addition. An increase in the amount of immobilized enzyme preparation added gave a 100% ester yield in 3 h. The immobilized preparation was quite stable, giving a 100% yield of ethyl-oleate during 11 repeated reactions, and 50% yield after 24 reactions. These results suggest that the lipase of our strain of B. cepacia LTEB11 immobilized on Accurel has good potential for application in biocatalysis in organic media.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5dbc648f2c7b02a8e9420b009df7e49a https://doi.org/10.1080/10242420701568674 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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