Abstract
Magnetic nanoparticles (MNp) Fe3O4 were prepared by chemical coprecipitation, and introduced onto collagen fibers to form magnetic collagen support (MNp-Col) for enzyme immobilization. Candida rugosa lipase has been successfully immobilized on MNp-Col supports by a covalent bond cross-linking agent, glutaraldehyde. The characteristics of MNp-Col and the immobilized lipase were investigated. The immobilized lipase displayed sound magnetic separation abilities in both aqueous and organic media. The activity of the immobilized lipase reached 2390 U/g under optimal conditions. The MNp-Col immobilized lipase shows broadened temperature and pH ranges for hydrolysis of olive oil emulsion. For synthesis of butyrate esters in an n-hexane medium, the yield changes through use of different alcohols, among which, butyric butyrate showed the highest yield. The prepared magnetic collagen fiber provides separation support for enzyme immobilization and has the potential to be used in other biotechnology fields.
Highlights
Enzymes are broadly used as ‘green’ biocatalysts in many fields because enzymatic reactions are normally carried out at mild conditions with high efficiency and specificity [1]
This indicates that the introduction of Fe3 O4 particles led to an increase of pore volume and a rougher surface of collagen fiber, while the immobilizing of lipase onto the magnetic supports caused a slight decrease of pore volume
The average pore sizes of native collagen, Magnetic nanoparticles (MNp)-Col and MNp-Col-IL, are approximately 13.70, 10.47, and 14.65 nm, respectively. This shows that the pores in collagen fiber supports and MNp-Col-IL fall into the mesopore size range [21]
Summary
Enzymes are broadly used as ‘green’ biocatalysts in many fields because enzymatic reactions are normally carried out at mild conditions with high efficiency and specificity [1]. Several shortcomings such as high cost, unstability to thermal or chemical, and non-reusability have restricted the application of free enzymes [2,3,4]. Enzyme immobilization has been reported as a valuable alternative since it permits the reuse of enzymes, and improves some other critical properties like activity, inhibition by reaction products, and selectivity [5]. The performances of immobilized lipases rely on the immobilization techniques and the chemical property of the support as well [6]. Different natural polymers have been employed for lipase immobilization such as agarose, alginate, chitosan, cellulose, and starch [11,12]
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