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      Immobilisation of cyclodextrin glucanotransferase into polyvinyl alcohol (PVA) nanofibres via electrospinning

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          Highlights

          • Fabrication of enzyme-carrying polymeric nanofibers by electrospinning.

          • PVA nanofibers structure and size were not affected by the addition of enzyme.

          • The electrospun CGTase/PVA nanofibers show excellent immobilisation efficiency.

          Abstract

          Immobilisation of cyclodextrin glucanotransferase (CGTase) on nanofibres was demonstrated. CGTase solution (1% v/v) and PVA (8 wt%) solution were mixed followed by electrospinning (−9 kV, 3 h). CGTase/PVA nanofibres with an average diameter of 176 ± 46 nm were successfully produced. The nanofibres that consist of immobilised CGTase were crosslinked with glutaraldehyde vapour. A CGTase/PVA film made up from the same mixture and treated the same way was used as a control experiment. The immobilised CGTase on nanofibres showed superior performance with nearly a 2.5 fold higher enzyme loading and 31% higher enzyme activity in comparison with the film.

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          Most cited references25

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          Cyclodextrins and their uses: a review

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            Immobilised enzymes: carrier-bound or carrier-free?

            Recent advances have been made in the development of carrier-free immobilised enzymes and several criteria established for the selection of immobilised enzymes for biotransformations. The pros and cons of carrier-free versus carrier-bound immobilised enzymes and of each type of carrier-free enzyme are discussed.
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              Enzyme-carrying polymeric nanofibers prepared via electrospinning for use as unique biocatalysts.

              Improvement of catalytic efficiency of immobilized enzymes via materials engineering was demonstrated through the preparation of bioactive nanofibers. Bioactive polystyrene (PS) nanofibers with a typical diameter of 120 nm were prepared and examined for catalytic efficiency for biotransformations. The nanofibers were produced by electrospinning functionalized PS, followed by the chemical attachment of a model enzyme, alpha-chymotrypsin. The observed enzyme loading as determined by active site titration was up to 1.4% (wt/wt), corresponding to over 27.4% monolayer coverage of the external surface of nanofibers. The apparent hydrolytic activity of the nanofibrous enzyme in aqueous solutions was over 65% of that of the native enzyme, indicating a high catalytic efficiency as compared to other forms of immobilized enzymes. Furthermore, nanofibrous alpha-chymotrypsin exhibited a much-improved nonaqueous activity that was over 3 orders of magnitude higher than that of its native counterpart suspended in organic solvents including hexane and isooctane. It appeared that the covalent binding also improved the enzyme's stability against structural denaturation, such that the half-life of the nanofibrous enzyme in methanol was 18-fold longer than that of the native enzyme.
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                Author and article information

                Contributors
                Journal
                Biotechnol Rep (Amst)
                Biotechnol Rep (Amst)
                Biotechnology Reports
                Elsevier
                2215-017X
                09 March 2016
                June 2016
                09 March 2016
                : 10
                : 44-48
                Affiliations
                [a ]Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, Japan
                [b ]Biotechnology Research Institute, Universiti Malaysia Sabah, 88400, Kota Kinabalu, Sabah, Malaysia
                [c ]Department of Process and Food Engineering, Faculty of Engineering, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia
                [d ]Department of Chemical Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, Japan
                [e ]Faculty of Chemical Engineering, Universiti Teknologi MARA, 40450 Shah Alam, Selangor, Malaysia
                [f ]Advanced Institute for Materials Research, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, 980-8577, Japan
                Author notes
                [* ]Corresponding author. mohdnazli@ 123456upm.edu.my
                Article
                S2215-017X(16)30010-8
                10.1016/j.btre.2016.03.003
                5040860
                618a652a-fa59-49f8-b1e8-6ea0ae090e6d
                © 2016 The Authors

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                : 5 January 2016
                : 7 March 2016
                : 7 March 2016
                Categories
                Article

                nanofibres,immobilisation,cgtase,electrospinning,cyclodextrins

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