Background
Type: Article

Improvement of stability and reusability of α-amylase immobilized on naringin functionalized magnetic nanoparticles: A robust nanobiocatalyst

Journal: International Journal of Biological Macromolecules (01418130)Year: 1 July 2018Volume: 113Issue: Pages: 354 - 360
Defaei M.Taheri Kafrani A.aMiroliaei M.a Yaghmaei P.
DOI:10.1016/j.ijbiomac.2018.02.147Language: English

Abstract

Enzyme immobilized on magnetic nanoparticles (MNPs) can be used as efficient recoverable biocatalysts under strong magnetic responses. In the present work, α-amylase was immobilized onto naringin functionalized MNPs via ionic interactions. For this purpose, the MNPs were functionalized with naringin, as a biocompatible flavonoid. The morphology, structure, and properties of functionalized MNPs and the immobilization of α-amylase on synthesized nanocomposite were characterized through different analytical tools including TGA, VSM, FTIR, SEM-EDX and TEM. Furthermore, the optimum conditions of temperature, pH, reaction time and enzyme concentration for immobilization process were investigated. The results showed that the optimal conditions for immobilization of α-amylase onto synthesized nanocarrier occurred at pH 6.5 and 55 °C. The reusability experiments revealed high activity maintenance of immobilized α-amylase even after 10 reaction cycles. Moreover, the storage stability of immobilized enzyme improved via immobilization in comparison with free one and it maintained 60% of its initial activity after 6 weeks storage at 4 °C. The improvements in enzyme catalytic properties via immobilization made this nanobiocatalyst as a good candidate in bio-industrial applications. Furthermore, the synthesized nanocomposite would have the potential for practical applications in other and binary enzyme immobilization. © 2018 Elsevier B.V.


Author Keywords

ImmobilizationMagnetic nanoparticlesNaringinReusabilityα-Amylase

Other Keywords

alpha-AmylasesBacillus subtilisBiocatalysisEnzymes, ImmobilizedFlavanonesHydrogen-Ion ConcentrationIndustryKineticsMagnetite NanoparticlesTemperatureamylaseaurantiinflavonoidmagnetic nanoparticlenanocarriernanocompositeflavanone derivativeimmobilized enzymemagnetite nanoparticleArticlebiocompatibilitycatalysiscatalystchemical structureconcentration (parameters)controlled studyenergy dispersive X ray spectroscopyenzyme activityenzyme immobilizationenzyme stabilityinfrared spectroscopymagnetometrymolecular interactionnanobiocatalystpHreaction timerecyclingstoragestorage temperaturethermogravimetrytransmission electron microscopychemistryenzymologymetabolism