Synthesis of glycinamides using protease immobilized magnetic nanoparticles
Autor: | Mayur R. Ladole, Abha Sahu, Pallavi Badhe, Ravindra V. Adivarekar, Aniruddha B. Pandit |
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Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
Thermogravimetric analysis
Immobilized enzyme lcsh:Biotechnology medicine.medical_treatment 02 engineering and technology Bacillus subtilis 010402 general chemistry 01 natural sciences Applied Microbiology and Biotechnology Article Immobilization Response surface methodology lcsh:TP248.13-248.65 medicine Organic chemistry Thermal stability Fourier transform infrared spectroscopy Protease biology Chemistry 021001 nanoscience & nanotechnology biology.organism_classification equipment and supplies 0104 chemical sciences Glycinamides Magnetic nanoparticles 0210 nano-technology Biotechnology Nuclear chemistry |
Zdroj: | Biotechnology Reports Biotechnology Reports, Vol 12, Iss C, Pp 13-25 (2016) |
ISSN: | 2215-017X |
Popis: | Highlights • Protease producing Bacillus subtilis was isolated from animal slaughter house waste. • Protease was covalently immobilized on amino-functionalized magnetic nanoparticles (AMNPs). • To our knowledge, for the first time these magnetic nano biocatalyst was used for the synthesis of series of novel glycinamides. • Parameters for glycinamides synthesis such as, pH, temperature and time were optimized using Response Surface Methodology. • Reusability study showed that protease immobilized MNPs retain up to 70% of initial activity after 8th cycles of reuse for the synthesis. 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. |
Databáze: | OpenAIRE |
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