Highly active biocatalyst for transesterification: Cross linked enzyme aggregates of Thermomyces lanuginosus and Candida antarctica B

Authors


Correspondence: Dr. Sigurd Schober, Renewable Resources Group, Institute of Chemistry, University of Graz, Heinrichstraße 28, 8010 Graz, Austria

E-mail: si.schober@uni-graz.at

Fax: 43 316 380 9840

Abstract

The preparation of cross-linked enzyme aggregates (CLEAs) with albumin as an additive is demonstrated successfully with lipase Thermomyces lanuginosus (TL) and lipase B of Candida antarctica (CalB). Investigations regarding the albumin admixture and the temperature optimum are employed. Compared to non-cross-linked lipase, CalB delivers the best results at a mass ratio of 1:16 lipase/albumin, which leads to a 24-fold increase of activity; TL at a mass ratio of 1:12, which leads to a eightfold increased activity. A transesterification yield of 61% m/m ethyl ester can be reached with 2.5% m/m CLEAs of lipase TL applied on rapeseed oil within 1.5 h reaction time. A catalyst mass of 10% m/m yields 94% m/m ethyl ester in the same time. Within six cycles of reuse, the catalyst remains stable. CLEAs of CalB and Novozym 435 (a commercial immobilized lipase B of C. antarctica) show comparable rates in ethanolysis and glycerolysis reaction.

Practical applications: CLEAs have become of increasing interest in terms of synthesis of organic compounds via bio-catalytic (green) approaches. The findings presented here are targeting at transesterification of fats and oils into corresponding alkyl esters applicable, e.g., as alternative fuel substitutes. High conversion rates coupled with hyperactivation effects as well as highly appealing reusability behavior indicate the practical benefits even for technical applications. Conversion of lipids into derivatives by CLEAs as demonstrated here, might extend utilization and conversion possibilities of biomass.

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