Covalent immobilization of peanut β-amylase for producing industrial nano-biocatalysts: A comparative study of kinetics, stability and reusability of the immobilized enzyme.

Abstract:

:Stability of enzymes is an important parameter for their industrial applicability. Here, we report successful immobilization of β-amylase (bamyl) from peanut (Arachis hypogaea) onto Graphene oxide-carbon nanotube composite (GO-CNT), Graphene oxide nanosheets (GO) and Iron oxide nanoparticles (Fe3O4). The Box-Behnken Design of Response Surface Methodology (RSM) was used which optimized parameters affecting immobilization and gave 90%, 88% and 71% immobilization efficiency, respectively, for the above matrices. β-Amylase immobilization onto GO-CNT (bamyl@GO-CNT) and Fe3O4 (bamyl@Fe3O4), resulted into approximately 70% retention of activity at 65 °C after 100 min of exposure. We used atomic force microscopy (AFM), scanning and transmission electron microscopy (SEM and TEM), Fourier transformed infrared (FT-IR) spectroscopy and fluorescence microscopy for characterization of free and enzyme bound nanostructures (NS). Due to the non-toxic nature of immobilization matrices and simple but elegant immobilization procedure, these may have potential utility as industrial biocatalysts for production of maltose.

journal_name

Food Chem

journal_title

Food chemistry

authors

Das R,Talat M,Srivastava ON,Kayastha AM

doi

10.1016/j.foodchem.2017.10.092

subject

Has Abstract

pub_date

2018-04-15 00:00:00

pages

488-499

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(17)31732-6

journal_volume

245

pub_type

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