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

There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

Abstract

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.

Related collections

Most cited references 42

Record: found
Abstract: not found
Article: not found

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Marion Bradford (1976)

0 comments Cited 8734 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: not found
Article: not found

Improvement of enzyme activity, stability and selectivity via immobilization techniques

César Mateo, Jose Palomo, Gloria Fernandez-Lorente … (2007)

0 comments Cited 290 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

Potential applications of enzymes immobilized on/in nano materials: A review.

Shakeel Ahmed Ansari, Qayyum Husain (2012)

Several new types of carriers and technologies have been implemented in the recent past to improve traditional enzyme immobilization which aimed to enhance enzyme loading, activity and stability to decrease the enzyme biocatalyst cost in industrial biotechnology. These include cross-linked enzyme aggregates, microwave-assisted immobilization, click chemistry technology, mesoporous supports and most recently nanoparticle-based immobilization of enzymes. The union of the specific physical, chemical, optical and electrical properties of nanoparticles with the specific recognition or catalytic properties of biomolecules has led to their appearance in myriad novel biotechnological applications. They have been applied time and again for immobilization of industrially important enzymes with improved characteristics. The high surface-to-volume ratio offered by nanoparticles resulted in the concentration of the immobilized entity being considerably higher than that afforded by experimental protocols based on immobilization on planar 2-D surfaces. Enzymes immobilized on nanoparticles showed a broader working pH and temperature range and higher thermal stability than the native enzymes. Compared with the conventional immobilization methods, nanoparticle based immobilization served three important features; (i) nano-enzyme particles are easy to synthesize in high solid content without using surfactants and toxic reagents, (ii) homogeneous and well defined core-shell nanoparticles with a thick enzyme shell can be obtained, and (iii) particle size can be conveniently tailored within utility limits. In addition, with the growing attention paid to cascade enzymatic reaction and in vitro synthetic biology, it is possible that co-immobilization of multi-enzymes could be achieved on these nanoparticles. Copyright Â© 2011 Elsevier Inc. All rights reserved.