Abstract
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.
Highlights
The industrial use of enzymes has continued to grow over recent years, but their utilization in many commercial applications is limited by rapid loss of catalytic activity, affected by even slight changes to their optimal operational conditions [1]
Spongin-based scaffolds were used for the first time as a support for the immobilization of lipase B from C. antarctica
MAS NMR were used to prove the immobilization of the lipase, and to determine the mechanism by which this enzyme is attached to the spongin surface, which is most probably based on hydrogen bonds
Summary
The industrial use of enzymes has continued to grow over recent years, but their utilization in many commercial applications is limited by rapid loss of catalytic activity, affected by even slight changes to their optimal operational conditions [1]. Methods based on the adsorption of biocatalysts on the matrix surface are simple and the most widely applied. This might be explained by the fact that there are insignificant conformational changes in the structure of the enzyme and its active sites, catalytic activity is maintained at a high level [8,9]. An additional benefit of this method is that the matrix may be formed by a very broad group of materials of various origins, ranging from inorganic compounds via synthetic up to organic materials obtained from natural sources [10,11]
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