Enzymatic esterification of fatty acid esters by tetraethylammonium amino acid ionic liquids-coated Candida rugosa lipase

[Display omitted] ► New tetraethylammonium amino acids ILs were used as a modifier with Candida rugosa lipase to produce two new biocatalysts (ILs-CRL). ► The activity of ILs-CRL was determined through esterification of oleyl alcohol with different fatty acids. ► The ILs-CRL system showed higher act...

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Bibliographic Details
Published in:Journal of molecular catalysis. B, Enzymatic Vol. 79; pp. 61 - 65
Main Authors: Abdul Rahman, Mohd Basyaruddin, Jumbri, Khairulazhar, Mohd Ali Hanafiah, Nurul Ain, Abdulmalek, Emilia, Tejo, Bimo Ario, Basri, Mahiran, Salleh, Abu Bakar
Format: Journal Article
Language:English
Published: Amsterdam Elsevier B.V 01-07-2012
Elsevier
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Summary:[Display omitted] ► New tetraethylammonium amino acids ILs were used as a modifier with Candida rugosa lipase to produce two new biocatalysts (ILs-CRL). ► The activity of ILs-CRL was determined through esterification of oleyl alcohol with different fatty acids. ► The ILs-CRL system showed higher activity on short, medium and long chain fatty acids compared to native CRL. ► Hydrophilicity of ILs may play an important role to stabilize the ILs-CRL. Enzymatic production of fatty acid esters from the esterification of oleyl alcohol with various fatty acids was investigated by using two new tetraethylammonium amino acid ionic liquids-coated Candida rugosa lipase (ILs-CRL) as biocatalysts in hexane. Both enzyme derivatives were prepared by mixing Candida rugosa lipase with tetraethylammonium l-histidinate (IL1) and tetraethylammonium l-asparaginate (IL2). The ILs-CRL system containing the equivalent protein concentration as in CRL showed higher esterification activity especially on medium chain fatty acids (C12–C16) as compared to non-coated CRL. Hydrophilicity of ILs may play an important role in hydrogen bonding with enzyme surface and consequently stabilize the ILs-CRL.
Bibliography:http://dx.doi.org/10.1016/j.molcatb.2012.03.003
ISSN:1381-1177
1873-3158
DOI:10.1016/j.molcatb.2012.03.003