Enzymes and protein's immobilization on magnetic nano supports is emerging as a promising candidate in the food, medical field, and areas of environmental studies. This work presents a study on purifiedBacillus thermoamylovoranslipase (BTL) by utilizing tetraethoxysilane (TEOS)-modified magnesium nano ferrite (MgNF) of 20 nm size. Its structural and morphological studies were investigated by powder X-ray diffractometry, high-resolution transmission electron microscopy, etc. Binding of BTL with MgNF was supported by using Fourier transform infrared spectroscopy. Magnetic behavior was examined by the vibrational sample magnetometer and Mossbauer spectrometer graphs. The enzymatic activity of BTL before and after immobilization was studied at different temperatures and reaction time. As per the Lineweaver-Burk plot, immobilized lipase has more biological affinity for fatty acids in comparison to the free lipase, and K(max)values of immobilized and free BTL were computed as 6.6 and 7.5 mM respectively, with excellent reusability(> 50%) even till 13 consecutive assay runs.