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.
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 m ) and was comparatively more stable in presence of some solvents (ethyl acetate, acetone, acetonitrile), metal ions (Ag + , Zn 2+ ) and β-mercaptoethanol. AlOP-ASNase was reused in a glass column reactor for l-asparagine hydrolysis upto nine successive cycles without any loss in activity. The AlOP-ASNase was effective in lowering l-asparagine level in blanched potato chips indicating its potential use in mitigating acrylamide formation in starchy foods. This cost-effective enzyme preparation had shelf-life of more than 30days and can be effectively used in starch based food industries.
(Copyright © 2018 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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