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Abstract: Hybrid nanoflowers materials have recently received great attention in enzyme immobilization applications because of the advantages such as their large surface area, excellent stability, simple, eco-friendly, and cost-effective synthesis. In this study, l-asparaginase which is an important commercial enzyme in the medicine and food industry was selected as a model enzyme. To the best of our knowledge, this study is the first report of designing l-asparaginase@hybrid nanoflowers to enhance its enzymatic performance. l-asparaginase@hybrid nanoflowers were synthesized using ASNase as an organic component and Cu(II) ion as inorganic component. They were characterized by their morphology and chemical point of view by using different techniques. The synthesized l-asparaginase@hybrid nanoflowers exhibited high residual activity at broad pH and high temperature ranges in comparison to free form. Moreover, l-asparaginase@hybrid nanoflowers possessed good reusability and excellent long-time storage stability. Especially, l-asparaginase@hybrid nanoflowers-3 maintained nearly 51 and 75% of its original activity, respectively, after nine consecutive catalytic cycles and storage at 30 °C for 4 weeks. The results indicated that these hybrid nanoflowers will be promising carrier matrix for the immobilization of ASNase in biotechnological applications with improved catalytic properties. Graphic Abstract: [Figure not available: see fulltext.] © 2020, Springer Science+Business Media, LLC, part of Springer Nature. |
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