The acyltransferase activity of lipase CAL‐A allows efficient fatty acid esters formation from plant oil even in an aqueous environment. Issue 12 (24th August 2015)
- Record Type:
- Journal Article
- Title:
- The acyltransferase activity of lipase CAL‐A allows efficient fatty acid esters formation from plant oil even in an aqueous environment. Issue 12 (24th August 2015)
- Main Title:
- The acyltransferase activity of lipase CAL‐A allows efficient fatty acid esters formation from plant oil even in an aqueous environment
- Authors:
- Müller, Janett
Sowa, Miriam A.
Dörr, Mark
Bornscheuer, Uwe T. - Abstract:
- Abstract : The enzymatic synthesis of fatty acid esters (FAE) can be performed by lipases in reaction systems in the absence of bulk water. However, some lipases such as Candida antarctica lipase A (CAL‐A) have an acyltransferase activity, which enables FAE synthesis from natural oils and suitable alcohols even in the presence of water. The ability to generate these compounds in an aqueous system would be interesting for an industrial application, because this could lead to a more cost‐efficient and environmentally friendly process as the alcohol donor also serves as solvent. Using refined palm kernel oil (PKO) the CAL‐A‐catalyzed ester synthesis was studied with methanol or ethanol in the presence of 5–10% (w/w) water. Optimizing reaction parameters (e.g., temperature and water content) resulted in up to 95% ester formation after 24 h. In addition, methanol allowed higher ester formation than ethanol. Practical applications: The enzymatic synthesis of fatty acid esters from plant oils using standard lipases is hampered by the fact that the presence of water leads to undesired formation of free fatty acids. The use of CAL‐A with its unique acyltransferase activity overcomes this limitation and hence makes the industrial scale synthesis of these esters more feasible. The identification of important parameters influencing the ester formation is crucial to establish such processes. Optimization of reaction conditions leads to protocols suitable to use lipase CAL‐A in a waterAbstract : The enzymatic synthesis of fatty acid esters (FAE) can be performed by lipases in reaction systems in the absence of bulk water. However, some lipases such as Candida antarctica lipase A (CAL‐A) have an acyltransferase activity, which enables FAE synthesis from natural oils and suitable alcohols even in the presence of water. The ability to generate these compounds in an aqueous system would be interesting for an industrial application, because this could lead to a more cost‐efficient and environmentally friendly process as the alcohol donor also serves as solvent. Using refined palm kernel oil (PKO) the CAL‐A‐catalyzed ester synthesis was studied with methanol or ethanol in the presence of 5–10% (w/w) water. Optimizing reaction parameters (e.g., temperature and water content) resulted in up to 95% ester formation after 24 h. In addition, methanol allowed higher ester formation than ethanol. Practical applications: The enzymatic synthesis of fatty acid esters from plant oils using standard lipases is hampered by the fact that the presence of water leads to undesired formation of free fatty acids. The use of CAL‐A with its unique acyltransferase activity overcomes this limitation and hence makes the industrial scale synthesis of these esters more feasible. The identification of important parameters influencing the ester formation is crucial to establish such processes. Optimization of reaction conditions leads to protocols suitable to use lipase CAL‐A in a water containing system for the synthesis of fatty acid methyl or ethyl esters in up to 95% concentration. Abstract : Optimization of reaction conditions leads to protocols suitable to use lipase CAL‐A in a water containing system for the synthesis of fatty acid methyl or ethyl esters in up to 95% concentration. … (more)
- Is Part Of:
- European journal of lipid science and technology. Volume 117:Issue 12(2015:Dec.)
- Journal:
- European journal of lipid science and technology
- Issue:
- Volume 117:Issue 12(2015:Dec.)
- Issue Display:
- Volume 117, Issue 12 (2015)
- Year:
- 2015
- Volume:
- 117
- Issue:
- 12
- Issue Sort Value:
- 2015-0117-0012-0000
- Page Start:
- 1903
- Page End:
- 1907
- Publication Date:
- 2015-08-24
- Subjects:
- Acyltransferase -- Alcohol -- CAL‐A -- Transesterification -- Water content
Oils and fats, Edible -- Periodicals
Lipids -- Periodicals
660.63 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1438-9312 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/ejlt.201500292 ↗
- Languages:
- English
- ISSNs:
- 1438-7697
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3829.730975
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 14467.xml