•Cellulase was immobilized on carbodiimide-activated surface of MWCNTs.•The bionanoconjugates were thermally more stable.•The t1/2 of bionanoconjugates was increased by four fold as compared to free cellulase.•The preparation could be reused ten times without significant loss in enzyme activity. In present study, Aspergillus niger cellulase was immobilized onto functionalized multiwalled carbon nanotubes (MWCNTs) via carbodiimide coupling. MWCNTs offer unique advantages including enhanced electronics properties, a large edge to basal plane ratio, rapid electrode kinetics and it’s possess higher tensile strength properties due to their structural arrangements. The immobilization was confirmed by FTIR (Fourier transform infrared spectroscopy) and SEM (scanning electron microscope). The bionanoconjugates prepared under optimized condition retained 85% activity with improved pH and thermal stability. The t1/2 of immobilized cellulase at 70 °C was four fold higher than free enzyme. The Km value indicates that affinity of bionanoconjugates towards substrate has increased by two times. The preparation could be reused ten times without much loss in enzyme activity. The enhanced catalytic efficiency, stability and reusability makes it useful for efficient cellulose hydrolysis.