Endo‐ and exo‐inulinases: Enzyme‐substrate interaction and rational immobilization |
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| Authors: | Alessandra Basso Patrizia Spizzo Valerio Ferrario Lorena Knapic Nina Savko Paolo Braiuca Cynthia Ebert Emanuele Ricca Vincenza Calabrò Lucia Gardossi |
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| Institution: | 1. Laboratory of Applied and Computational Biocatalysis, Dipartimento di Scienze Farmaceutiche, Università degli Studi di Trieste, Piazzale Europa, Trieste 1‐34127, Italy;2. SPRIN s.r.l., c/o Università degli Studi di Trieste, Piazzale Europa, Trieste 1‐34127, Italy;3. Dipartimento di Ingegneria Chimica e dei Materiali, Università della Calabria, via P. Bucci, Edificio Cubo 44A, Arcavacata di Rende 87036, Italy |
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| Abstract: | Three‐dimensional models of exoinulinase from Bacillus stearothermophilus and endoinulinase from Aspergillus niger were built up by means of homology modeling. The crystal structure of exoinulinase from Aspergillus awamori was used as a template, which is the sole structure of inulinase resolved so far. Docking and molecular dynamics simulations were performed to investigate the differences between the two inulinases in terms of substrate selectivity. The analysis of the structural differences between the two inulinases provided the basis for the explanation of their different regio‐selectivity and for the understanding of enzyme‐substrate interactions. Surface analysis was performed to point out structural features that can affect the efficiency of enzymes also after immobilization. The computational analysis of the three‐dimensional models proved to be an effective tool for acquiring information and allowed to formulate an optimal immobilized biocatalyst even more active that the native one, thus enabling the full exploitation of the catalytic potential of these enzymes. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2010 |
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| Keywords: | Endo‐inulinase exo‐inulinase inulin molecular modeling docking homology modeling immobilization |
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