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Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil: The impact of support functionalization on lipase activity, selectivity and stability
- Source :
- International Journal of Biological Macromolecules. 108:674-686
- Publication Year :
- 2018
- Publisher :
- Elsevier BV, 2018.
-
Abstract
- The objective of this paper was to carry out an integral study of the use of hydrophobic chitosan as a low-cost support for immobilizing lipases and their further application in the selective hydrolysis of fish oil. Chitosan functionalized with different alkyl chains (C4, C8, C12) were characterized by FTIR, TGA, SEM, and Rose Bengal adsorption. Lipase B from Candida antarctica (CalB) and lipase from Rhizomucor miehei (RML) were immobilized obtaining a higher expressed activity at a longer alkyl chain length of support. Biocatalyst thermal stability showed that the impact of the alkyl chain length on enzyme stabilization varied according to the lipase source. The biocatalysts were applied in menhaden oil hydrolysis. Total polyunsaturated fatty acids released after 30 h of reaction with lipases immobilized in butyl, octyl and dodecyl-chitosan was 60, 107, and 90 mM for CalB biocatalysts, and 560, 392, and 50 mM for RML biocatalysts, respectively. Selectivity of CalB was not affected by the alkyl chain, while in the case of RML, a higher selectivity to cis-4,7,10,13,16,19-docohexaenoic acid release was obtained with dodecyl-chitosan. In conclusion, the adequate functionalization of chitosan varied according to lipase source, affecting their activity, stability and performance in the hydrolysis of fish oil.
- Subjects :
- Models, Molecular
Molecular Conformation
Triacylglycerol lipase
Rhizomucor miehei
02 engineering and technology
01 natural sciences
Biochemistry
Substrate Specificity
Chitosan
Structure-Activity Relationship
chemistry.chemical_compound
Hydrolysis
Fish Oils
Structural Biology
Enzyme Stability
Spectroscopy, Fourier Transform Infrared
Organic chemistry
Lipase
Molecular Biology
Alkyl
chemistry.chemical_classification
Molecular Structure
biology
010405 organic chemistry
General Medicine
Enzymes, Immobilized
equipment and supplies
021001 nanoscience & nanotechnology
biology.organism_classification
0104 chemical sciences
Enzyme Activation
chemistry
Biocatalysis
biology.protein
Thermodynamics
Candida antarctica
0210 nano-technology
Selectivity
Hydrophobic and Hydrophilic Interactions
Subjects
Details
- ISSN :
- 01418130
- Volume :
- 108
- Database :
- OpenAIRE
- Journal :
- International Journal of Biological Macromolecules
- Accession number :
- edsair.doi.dedup.....98e4146e5fa76b3140b06dee6e7444cf
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2017.12.062