Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization

The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed...

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Bibliographic Details
Published in:Catalysts 2017-05, Vol.7 (5), p.147
Main Authors: Zdarta, Jakub, Norman, Małgorzata, Smułek, Wojciech, Moszyński, Dariusz, Kaczorek, Ewa, Stelling, Allison, Ehrlich, Hermann, Jesionowski, Teofil
Format: Article
Language:English
Subjects:
Biomass
Catalysis
Catalysts
Catalytic activity
Chemical reactions
Conversion
Corrosion resistance
Esters
Fatty acids
Fuels
Immobilization
Lipase
Methanol
Rapeseed
Rapeseed oil
Scaffolds
Storage stability
Transesterification
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Summary:The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed for the first time. Lipase B-containing biocatalytic system exhibited the highest catalytic activity retention (89%) after 60 min of immobilization at pH 7 and temperature of 4 °C. Immobilization was found to improve the thermal and chemical stability compared to free lipase, and retain over 80% of its initial catalytic activity over a wide range of temperature (30-60 °C) and pH (6-9). Additionally, immobilized lipase has good storage stability and retains over 70% of its initial activity even after catalyzing of 25 reaction cycles. The obtained product was used in a transesterification reaction of rapeseed oil with methanol and proved to be an efficient biocatalyst for biofuel production. The highest conversion value and fatty acids methyl esters (FAME) concentration were observed after a process conducted at 40 °C and pH 10. The possible mechanism of interaction between the enzyme and the spongin-based support is proposed and discussed.
ISSN:2073-4344
2073-4344
DOI:10.3390/catal7050147