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Endo‐ and exo‐inulinases: Enzyme‐substrate interaction and rational immobilization
Author(s) -
Basso Alessandra,
Spizzo Patrizia,
Ferrario Valerio,
Knapic Lorena,
Savko Nina,
Braiuca Paolo,
Ebert Cynthia,
Ricca Emanuele,
Calabrò Vincenza,
Gardossi Lucia
Publication year - 2009
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.334
Subject(s) - aspergillus awamori , inulinase , biocatalysis , homology modeling , docking (animal) , chemistry , rational design , aspergillus niger , selectivity , active site , enzyme , substrate (aquarium) , biochemistry , biology , catalysis , materials science , nanotechnology , medicine , ecology , ionic liquid , nursing
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