Suitability of recombinant lipase immobilised on functionalised magnetic nanoparticles for fish oil hydrolysis

Verma, Madan L, Rao, Nalam M, Tsuzuki, Takuya, Barrow, Colin J and Puri, Munish 2019, Suitability of recombinant lipase immobilised on functionalised magnetic nanoparticles for fish oil hydrolysis, Catalysts, vol. 9, no. 5, pp. 1-15, doi: 10.3390/catal9050420.

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Title Suitability of recombinant lipase immobilised on functionalised magnetic nanoparticles for fish oil hydrolysis
Author(s) Verma, Madan L
Rao, Nalam M
Tsuzuki, Takuya
Barrow, Colin JORCID iD for Barrow, Colin J orcid.org/0000-0002-2153-7267
Puri, MunishORCID iD for Puri, Munish orcid.org/0000-0003-2469-3326
Journal name Catalysts
Volume number 9
Issue number 5
Article ID 420
Start page 1
End page 15
Total pages 15
Publisher MDPI
Place of publication Basel, Switzerland
Publication date 2019-05
ISSN 2073-4344
Keyword(s) Magnetic
Covalent immobilisation
Recombinant enzyme
Structure characterisation
Fish oil
Omega-3 fatty acids
Science & Technology
Physical Sciences
Chemistry, Physical
Chemistry
Summary Recombinant Bacillus subtilis lipase was immobilised on magnetic nanoparticles by a facile covalent method and applied to fish oil hydrolysis. High loading of enzyme to the functionalised nanoparticle was achieved with a protein binding efficiency of 95%. Structural changes of the confined enzyme on the surface of the nanoparticles was investigated using transmission electron microscopy and spectroscopic techniques (attenuated total reflectance-Fourier transform infrared and circular dichroism). The biocatalytic potential of immobilised lipase was compared with that of free enzyme and biochemically characterised with respect to different parameters such as pH, temperature, substrate concentrations and substrate specificity. The thermal stability of functionalised nanoparticle bound enzyme was doubled that of free enzyme. Immobilised lipase retained more than 50% of its initial biocatalytic activity after recyclability for twenty cycles. The ability to the immobilised thermostable lipase to concentrate omega-3 fatty acids from fish oil was investigated. Using synthetic substrate, the immobilised enzyme showed 1.5 times higher selectivity for docosahexaenoic acid (DHA), and retained the same degree of selectivity for eicosapentaenoic acid (EPA), when compared to the free enzyme.
Language eng
DOI 10.3390/catal9050420
Indigenous content off
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2019, the authors
Persistent URL http://hdl.handle.net/10536/DRO/DU:30123757

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