Suitability of Recombinant Lipase Immobilised on Functionalised Magnetic Nanoparticles for Fish Oil Hydrolysis

Catalysts

NalamM Rao¹  ColinJ Barrow²  Munish Puri²  MadanL Verma²  Takuya Tsuzuki³ 

[1] Centre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Hyderabad 500007, India;Centre for Chemistry and Biotechnology, Deakin University, Waurn Ponds, Geelong 3216, VIC, Australia;Research School of Engineering, Australian National University, Canberra 2601, ACT, Australia;

关键词: magnetic;    covalent immobilisation;    recombinant enzyme;    structure characterisation;    fish oil;    omega-3 fatty acids;   

DOI  :  10.3390/catal9050420

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown