title: Xylanase Immobilized on Novel Multifunctional Hyperbranched Polyglycerol-Grafted Magnetic Nanoparticles: An Efficient and Robust Biocatalyst.
abstract: Although several strategies are now available for immobilization of enzymes to magnetic nanoparticles for bioapplications, little progresses have been reported on the use of dendritic or hyperbranched polymers for the same purpose. Herein, we demonstrated synthesis of magnetic nanoparticles supported hyperbranched polyglycerol (MNP/HPG) and a derivative conjugated with citric acid (MNP/HPG-CA) as unique and convenient nanoplatforms for immobilization of enzymes. Then, an important industrial enzyme, xylanase, was immobilized on the nanocarriers to produce robust biocatalysts. A variety of analytical tools were used to study the morphological, structural, and chemical properties of the biocatalysts. Additionally, the results of biocatalyst systems exhibited the substantial improvement of reactivity, reusability, and stability of xylanase due to this strategy, which might confer them a wider range of applications.
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Amir
authors.initials: A
authors.lastname: Landarani-Isfahani
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Asghar
authors.initials: A
authors.lastname: Taheri-Kafrani
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Mina
authors.initials: M
authors.lastname: Amini
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Valiollah
authors.initials: V
authors.lastname: Mirkhani
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Majid
authors.initials: M
authors.lastname: Moghadam
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Asieh
authors.initials: A
authors.lastname: Soozanipour
authors.affiliation: Catalysis Division, Department of Chemistry, and ‡Department of Biotechnology, Faculty of Advanced Sciences and Technologies, University of Isfahan , Isfahan 81746-73441, Iran.
authors.forename: Amir
authors.initials: A
authors.lastname: Razmjou
mesh_terms: D001203:Ascomycota / Q000201:enzymology*; D002384:Catalysis; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D060526:Magnetic Fields; D053758:Nanoparticles / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry*
chemical_list: D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011092:Polyethylene Glycols; D043364:Endo-1,4-beta Xylanases; C000595209:polyethylene glycol 1000