Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as Cross-linked enzyme aggregates (CLEAs)

Autor:	Funda Kartal, Frank Hollmann, Roger A. Sheldon, Ali Kılınç, Michiel Janssen
Rok vydání:	2011
Předmět:	Chromatography Ethanol Immobilized enzyme biology Cyclohexane Chemistry Process Chemistry and Technology Bioengineering Biochemistry Catalysis Candida rugosa chemistry.chemical_compound biology.protein Organic chemistry Leaching (metallurgy) Glutaraldehyde Lipase
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 71:85-89
ISSN:	1381-1177
DOI:	10.1016/j.molcatb.2011.04.002
Popis:	Cross-linked enzyme aggregates (CLEA (R) s) were prepared from Candida rugosa lipase (CrL) using glutaraldehyde as the cross-linker. The optimum conditions of the immobilization process were determined (precipitant: ethanol, crosslinker concentration: 25 mM, enzyme concentration: 50 mg/ml, crosslinking time: 45 min.). CLEAs were shown to have several advantages compared to the free enzyme. They were more stable at 50 degrees C and 60 degrees C and had good reusability; retaining 40% of their initial activity after 15 recycles in aqueous media and remaining constant at that level thereafter, suggesting some initial leaching in water. The CLEAs catalyzed esterification reactions in cyclohexane, affording higher conversions than with the free enzyme, especially when longer fatty acids and alcohols were used as substrates. (C) 2011 Elsevier B.V. All rights reserved.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54502a681eddaeb8f6311754a0a6ab7d https://doi.org/10.1016/j.molcatb.2011.04.002 Zobrazit plný text záznamu Full Text from ScienceDirect