67
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Fructose Production by Inulinase Covalently Immobilized on Sepabeads in Batch and Fluidized Bed Bioreactor

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The present work is an experimental study of the performance of a recently designed immobilized enzyme: inulinase from Aspergillus sp. covalently immobilized on Sepabeads. The aim of the work is to test the new biocatalyst in conditions of industrial interest and to assess the feasibility of the process in a fluidized bed bioreactor (FBBR). The catalyst was first tested in a batch reactor at standard conditions and in various sets of conditions of interest for the process. Once the response of the catalyst to different operating conditions was tested and the operational stability assessed, one of the sets of conditions tested in batch was chosen for tests in FBBR. Prior to reaction tests, preliminary fluidization tests were realized in order to define an operating range of admissible flow rates. As a result, the FBR was run at different feed flow rates in a closed cycle configuration and its performance was compared to that of the batch system. The FBBR proved to be performing and suitable for scale up to large fructose production.

          Related collections

          Most cited references5

          • Record: found
          • Abstract: found
          • Article: not found

          Epoxy sepabeads: a novel epoxy support for stabilization of industrial enzymes via very intense multipoint covalent attachment.

          Sepabeads-EP (a new epoxy support) has been utilized to immobilize-stabilize the enzyme penicillin G acylase (PGA) via multipoint covalent attachment. These supports are very robust and suitable for industrial purposes. Also, the internal geometry of the support is composed by cylindrical pores surrounded by the convex surfaces (this offers a good geometrical congruence for reaction with the enzyme), and it has a very high superficial density of epoxy groups (around 100 micromol/mL). These features should permit a very intense enzyme-support interaction. However, the final stability of the immobilized enzyme is strictly dependent on the immobilization protocol. By using conventional immobilization protocols (neutral pH values, nonblockage of the support) the stability of the immobilized enzyme was quite similar to that achieved using Eupergit C to immobilize the PGA. However, when using a more sophisticated three-step immobilization/stabilization/blockage procedure, the Sepabeads derivative was hundreds-fold more stable than Eupergit C derivatives. The protocol used was as follows: (i) the enzyme was first covalently immobilized under very mild experimental conditions (e.g., pH 7.0 and 20 degrees C); (ii) the already immobilized enzyme was further incubated under more drastic conditions (higher pH values, long incubation periods, etc.) in order to "facilitate" the formation of new covalent linkages between the immobilized enzyme molecule and the support; (iii) the remaining epoxy groups of the support were blocked with very hydrophilic compounds to stop any additional interaction between the enzyme and the support. This third point was found to be critical for obtaining very stable enzymes: derivatives blocked with mercaptoethanol were much less stable than derivatives blocked with glycine or other amino acids. This was attributed to the better masking of the hydrophobicity of the support by the amino acids (having two charges).
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Recent developments in microbial inulinases. Its production, properties, and industrial applications.

            Microbial inulinases are an important class of industrial enzymes that have gained much attention recently. Inulinases can be produced by a host of microorganisms, including fungi, yeast, and bacteria. Among them, however, Aspergillus sp. (filamentous fungus) and Kluyveromyces sp. (diploid yeast) are apparently the preferred choices for commercial applications. Among various substrates (carbon source) employed for their production, inulin-containing plant materials offer advantages in comparison to pure substrates. Although submerged fermentation has been universally used as the technique of fermentation, attempts are being made to develop solid-state fermentation technology also. Inulinases catalyze the hydrolysis of inulin to D-fructose (fructose syrup), which has gained an important place in human diets today. In addition, inulinases are finding other newer applications. This article reviews more recent developments, especially those made in the past decade, on microbial inulinases--its production using various microorganisms and substrates. It also describes the characteristics of various forms of inulinases produced as well as their applications.
              Bookmark
              • Record: found
              • Abstract: not found
              • Book Chapter: not found

              Microbial Inulinases: Fermentation Process, Properties, and Applications

                Bookmark

                Author and article information

                Journal
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                Molecular Diversity Preservation International (MDPI)
                1422-0067
                19 March 2010
                2010
                : 11
                : 3
                : 1180-1189
                Affiliations
                [1 ]Department of Engineering Modeling, University of Calabria, I-87036 Arcavacata di Rende, CS, Italy; E-Mails: ericca@ 123456unical.it (E.R.) calabrov@ 123456unical.it (V.C.); gabriele.iorio@ 123456unical.it (G.I.)
                [2 ] SPRIN S.p.A., c/o BIC, Via Flavia 23/A, 34100 Trieste, Italy; E-Mail: basso@ 123456sprintechnologies.com
                [3 ]Laboratory of Applied and Computational Biocatalysis, Dipartimento di Scienze Farmaceutiche, Università degli Studi, P.le Europa 1, 34127 Trieste, Italy; E-Mail: gardossi@ 123456units.it
                Author notes
                [* ] Author to whom correspondence should be addressed; Tel.: +39-0984-49-6711; Fax: +39-0984-49-4706; E-Mail: stefano.curcio@ 123456unical.it .
                Article
                ijms-11-01180
                10.3390/ijms11031180
                2869238
                20480008
                3d3e4fd1-6042-441d-8721-1f2e9be0e1f0
                © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 13 January 2010
                : 17 March 2010
                Categories
                Article

                Molecular biology
                inulin hydrolysis,fructose,fluidized bed reactor,enzyme reaction
                Molecular biology
                inulin hydrolysis, fructose, fluidized bed reactor, enzyme reaction

                Comments

                Comment on this article