We report the statistical optimization of the immobilization of alkaline ${alpha}$-amylase [E.C. 3.2.1.1] from Bacillus alcalophilus onto nano-sized supermagnetic ironoxide nanoparticles (MNPs) for augmenting the cost effective industrial application of MNP-bound ${alpha}$-amylase. Both Plackett-Burman factorial design and response surface methodology (RSM) were employed to screen the influence of different parameters and the central effect of response on the ${alpha}$-amylase-iron oxide MNP binding process. The high coefficient of determination ($R^2$) and analysis of variance (ANOVA) of the quadratic model indicated the competence of the proposed model. The size of the MNPs was confirmed by X-ray diffraction and scanning electron microscope analyses in which Fourier transform infrared spectroscopy suggested immobilization of the enzyme on iron-oxide MNPs. A significant improvement (~ 26-fold) in specific activity, thermal and storage stability, and reusability of ${alpha}$-amylase after binding with iron-oxide MNP reinforced the improved biotechnological potential of the ${alpha}$-amylase iron-oxide MNP bioconjugate compared to free ${alpha}$-amylase. These results open new avenues for applying this MNP immobilized enzyme in different industrial sectors, notably in the paper and brewing industries.