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Synthesis of glycinamides using protease immobilized magnetic nanoparticles.


ABSTRACT: 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 2,2'((carboxymethyl) 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.

SUBMITTER: Sahu A 

PROVIDER: S-EPMC5361075 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Synthesis of glycinamides using protease immobilized magnetic nanoparticles.

Sahu Abha A   Badhe Pallavi Sharad PS   Adivarekar Ravindra R   Ladole Mayur Ramrao MR   Pandit Aniruddha Bhalchandra AB  

Biotechnology reports (Amsterdam, Netherlands) 20160920


In the present investigation, <i>Bacillus subtilis</i> 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. X  ...[more]

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