Catalytic characteristics and application of l-asparaginase immobilized on aluminum oxide pellets.
Autor: | Agrawal S; Enzyme Technology and Molecular Catalysis Laboratory, Department of Microbiology, Dr. Harisingh Gour Vishwavidyalaya (A Central University), Sagar, M.P. 470003, India., Sharma I; Enzyme Technology and Molecular Catalysis Laboratory, Department of Microbiology, Dr. Harisingh Gour Vishwavidyalaya (A Central University), Sagar, M.P. 470003, India., Prajapati BP; Enzyme Technology and Molecular Catalysis Laboratory, Department of Microbiology, Dr. Harisingh Gour Vishwavidyalaya (A Central University), Sagar, M.P. 470003, India., Suryawanshi RK; Enzyme Technology and Molecular Catalysis Laboratory, Department of Microbiology, Dr. Harisingh Gour Vishwavidyalaya (A Central University), Sagar, M.P. 470003, India., Kango N; Enzyme Technology and Molecular Catalysis Laboratory, Department of Microbiology, Dr. Harisingh Gour Vishwavidyalaya (A Central University), Sagar, M.P. 470003, India. Electronic address: nkango@gmail.com. |
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Jazyk: | angličtina |
Zdroj: | International journal of biological macromolecules [Int J Biol Macromol] 2018 Jul 15; Vol. 114, pp. 504-511. Date of Electronic Publication: 2018 Mar 21. |
DOI: | 10.1016/j.ijbiomac.2018.03.081 |
Abstrakt: | l-asparaginase from Escherichia coli (l-ASNase) was covalently immobilized on aluminum oxide pellets (AlOPs) using a cross-linking agent, glutaraldehyde. Maximum immobilization yield (85.0%) was obtained after optimizing immobilization parameters using response surface methodology (RSM). Both free and immobilized l-ASNase (AlOP-ASNase) were optimally active at 37°C and pH7.5. However, the bioconjugate exhibited enhanced activity and stability at different pH and temperatures. It had higher affinity (low K (Copyright © 2018 Elsevier B.V. All rights reserved.) |
Databáze: | MEDLINE |
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