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Immobilization of Inulinase on Aminated Multiwalled Carbon Nanotubes by Glutaraldehyde Cross-Linking for the Production of Fructose

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Abstract

In the present work, an attempt was made to enhance immobilization yield and operational stability of inulinase (Exo-II) from Penicillium oxalicum onto amino (+NH2) terminated multiwalled carbon nanotubes (MWCNTs) through glutaraldehyde (GA) cross-linking. A statistical study using response surface methodology (RSM) was employed to optimise inulinase immobilization onto 3-aminopropyl-triethoxysilane (APTES) and GA modified surfaces of MWCNTs. Under optimized conditions (APTES concentration 4%; sonication time 4 h; GA concentration 2%; GA activation time 75 min; enzyme load 27.5 IU and enzyme coupling time 2.75 h), inulinase activity and immobilization yield obtained were 73.9% and 84.9%, respectively. An increase in inulinase activity (1.22-fold) and immobilization yield (1.14-fold) was observed after modification of aminated MWCNTs by GA cross-linking. Developed immobilized biocatalyst shown excellent operational stability for 43 cycles for fructose production in a batch system. Increased immobilization yield and operational stability of the developed biocatalyst onto APTES-GA functionalized MWCNTs justifies it a good candidate for fructose production from inulin.

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Acknowledgements

Authors are thankful to the Head, Department of Biotechnology, Punjabi University, Patiala for availing necessary laboratory facilities to execute the present work.

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Authors and Affiliations

  1. Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala, Punjab, 147 002, India

    Ram Sarup Singh & Kanika Chauhan

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  1. Ram Sarup Singh
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  2. Kanika Chauhan
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Correspondence to Ram Sarup Singh.

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Singh, R.S., Chauhan, K. Immobilization of Inulinase on Aminated Multiwalled Carbon Nanotubes by Glutaraldehyde Cross-Linking for the Production of Fructose. Catal Lett 149, 2718–2727 (2019). https://doi.org/10.1007/s10562-019-02743-5

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  • DOI: https://doi.org/10.1007/s10562-019-02743-5

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