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      Immobilization of Peroxidase on Functionalized MWCNTs-Buckypaper/Polyvinyl alcohol Nanocomposite Membrane

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          Abstract

          Surface modified Multi-walled carbon nanotubes (MWCNTs) Buckypaper/Polyvinyl Alcohol (BP/PVA) composite membrane was synthesized and utilized as support material for immobilization of Jicama peroxidase (JP). JP was successfully immobilized on the BP/PVA membrane via covalent bonding by using glutaraldehyde. The immobilization efficiency was optimized using response surface methodology (RSM) with the face-centered central composite design (FCCCD) model. The optimum enzyme immobilization efficiency was achieved at pH 6, with initial enzyme loading of 0.13 U/mL and immobilization time of 130 min. The results of BP/PVA membrane showed excellent performance in immobilization of JP with high enzyme loading of 217 mg/g and immobilization efficiency of 81.74%. The immobilized system exhibited significantly improved operational stability under various parameters, such as pH, temperature, thermal and storage stabilities when compared with free enzyme. The effective binding of peroxidase on the surface of the BP/PVA membrane was evaluated and confirmed by Field emission scanning electron microscopy (FESEM) coupled with Energy Dispersive X-Ray Spectroscopy (EDX), Fourier transform infrared spectroscopy (FTIR) and Thermogravimetric Analysis (TGA). This work reports the characterization results and performances of the surface modified BP/PVA membrane for peroxidase immobilization. The superior properties of JP-immobilized BP/PVA membrane make it promising new-generation nanomaterials for industrial applications.

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          Enzyme immobilization: an overview on techniques and support materials

          The current demands of the world’s biotechnological industries are enhancement in enzyme productivity and development of novel techniques for increasing their shelf life. These requirements are inevitable to facilitate large-scale and economic formulation. Enzyme immobilization provides an excellent base for increasing availability of enzyme to the substrate with greater turnover over a considerable period of time. Several natural and synthetic supports have been assessed for their efficiency for enzyme immobilization. Nowadays, immobilized enzymes are preferred over their free counterpart due to their prolonged availability that curtails redundant downstream and purification processes. Future investigations should endeavor at adopting logistic and sensible entrapment techniques along with innovatively modified supports to improve the state of enzyme immobilization and provide new perspectives to the industrial sector.
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            Enzyme immobilization: an update.

            Compared to free enzymes in solution, immobilized enzymes are more robust and more resistant to environmental changes. More importantly, the heterogeneity of the immo-bilized enzyme systems allows an easy recovery of both enzymes and products, multiple re-use of enzymes, continuous operation of enzymatic processes, rapid termination of reactions, and greater variety of bioreactor designs. This paper is a review of the recent literatures on enzyme immobilization by various techniques, the need for immobilization and different applications in industry, covering the last two decades. The most recent papers, patents, and reviews on immobilization strategies and application are reviewed.
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              Immobilization of enzymes on porous silicas--benefits and challenges.

              Porous silica materials have extensively been used for the immobilization of enzymes aiming at their use as biocatalysts or biosensors. This tutorial review will discuss the benefits and challenges of different immobilization techniques and will provide references to recent papers for further reading. Moreover, novel trends and unsolved problems will be introduced.
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                Author and article information

                Contributors
                mubarak.mujawar@curtin.edu.my , mubarak.yaseen@gmail.com
                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group UK (London )
                2045-2322
                18 February 2019
                18 February 2019
                2019
                : 9
                : 2215
                Affiliations
                [1 ]Department of Chemical Engineering, Faculty of Engineering and Science, Curtin University, 98009 Sarawak, Malaysia
                [2 ]GRID grid.430718.9, Graphene & Advanced 2D Materials Research Group (GAMRG), School of Science and Technology, , Sunway University, No. 5, Jalan University, Bandar Sunway, ; 47500 Subang Jaya, Selangor Malaysia
                [3 ]ISNI 0000 0001 2296 1505, GRID grid.410877.d, Department of Chemical Process Engineering, , Malaysia-Japan International Institute of Technology (MJIIT) Universiti Teknologi Malaysia (UTM), ; Jalan Sultan Yahya Petra, 54100 Kuala Lumpur, Malaysia
                Author information
                http://orcid.org/0000-0001-7083-2521
                http://orcid.org/0000-0002-4547-8046
                Article
                39621
                10.1038/s41598-019-39621-4
                6379398
                30778111
                7cab1b40-576d-4a81-8297-dbd761df49cd
                © The Author(s) 2019

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 6 November 2018
                : 29 January 2019
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