چکیده (انگلیسی):

In the present investigation, Bacillus subtilis was isolated from slaughterhouse waste and screened for the
production of protease enzyme. The purified protease was successfully immobilized on magnetic
nanoparticles (MNPs) and used for the synthesis of series of glycinamides. The binding and thermal
stability of protease on MNPs was confirmed by FTIR spectroscopy and TGA analysis. The surface
morphology of MNPs before and after protease immobilization was carried out using SEM analysis. XRD
pattern revealed no phase change in MNPs after enzyme immobilization. The processing parameters for
glycinamides synthesis viz. temperature, pH, and time were optimized using Response Surface
Methodology (RSM) by using Design Expert (9.0.6.2). The maximum yield of various amides
2 butyramidoacetic acid (AMD-1,83.4%), 2-benzamidoacetic acid (AMD-2,80.5%) and 2,20((carboxy-
methyl) amino)-2-oxoethyl)-2-hydroxysuccinyl)bis(azanediyl))diacetic acid (AMD-3,80.8%) formed was
observed at pH-8, 50 C and 30 min. The synthesized immobilized protease retained 70% of the initial
activity even after 8 cycles of reuse.