Development of l -asparaginase@hybrid Nanoflowers (ASNase@HNFs) Reactor System with Enhanced Enzymatic Reusability and S
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Development of l‑asparaginase@hybrid Nanoflowers (ASNase@HNFs) Reactor System with Enhanced Enzymatic Reusability and Stability Samir Abbas Ali Noma1 · Burcu Somtürk Yılmaz2 · Ahmet Ulu1 · Nalan Özdemir2 · Burhan Ateş1 Received: 13 May 2020 / Accepted: 21 August 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
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.
* Nalan Özdemir [email protected] * Burhan Ateş [email protected] 1
Department of Chemistry, Faculty of Arts and Science, İnönü University, 44280 Malatya, Turkey
Department of Chemistry, Faculty of Science, Erciyes University, 38039 Kayseri, Turkey
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Graphic Abstract
Keywords Hybrid nanoflowers · Asparaginase · Enzyme immobilization · Improved stability
1 Introduction It is well known that the use of soluble enzymes in terms of industrial processes is hampered due to their low operational stability, non-reusability, and high cost [1]. Immobilization is one of the promising methods to overcome these major drawbacks [2]. Immobilization allows reuse, long-term storage and enables more easily separation from the reaction medium of enzyme [3]. Notwithstanding all these advantages if the appropriate carrier matrix and immobilization method are not selected, the catalytic activity of the immobilized enzyme may be suffering because of reduced mobility, unfavorable conformation and mass-transfer limitation [4]. Therefore, the carrier matrix and the immobilization method are two important factors determining the catalytic activity of the immobilized enzyme. Among promising carrier matrixes, protein-inorganic hybrid nanoflowers (HNFs) have recei
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