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Regioselective Deacetylation of Disaccharides via Immobilized Aspergillus niger Esterase(s)-catalyzed Hydrolysis in Aqueous and Non-aqueous Media

Authors

  • Dr. Teodora Bavaro,

    Corresponding author
    1. Department of Drug Sciences and Italian Biocatalysis Center, University of Pavia, Via Taramelli 12, 27100 Pavia (Italy), Fax: (+39) 0382-422975
    • Department of Drug Sciences and Italian Biocatalysis Center, University of Pavia, Via Taramelli 12, 27100 Pavia (Italy), Fax: (+39) 0382-422975
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  • Dr. Pamela Torres-Salas,

    1. Department of Drug Sciences and Italian Biocatalysis Center, University of Pavia, Via Taramelli 12, 27100 Pavia (Italy), Fax: (+39) 0382-422975
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  • Nicola Antonioli,

    1. Department of Drug Sciences and Italian Biocatalysis Center, University of Pavia, Via Taramelli 12, 27100 Pavia (Italy), Fax: (+39) 0382-422975
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  • Dr. Carlo F. Morelli,

    1. Department of Chemistry and Italian Biocatalysis Center, University of Milan, Via Golgi 19, 20133 Milan (Italy)
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  • Prof. Giovanna Speranza,

    1. Department of Chemistry and Italian Biocatalysis Center, University of Milan, Via Golgi 19, 20133 Milan (Italy)
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  • Prof. Marco Terreni

    1. Department of Drug Sciences and Italian Biocatalysis Center, University of Pavia, Via Taramelli 12, 27100 Pavia (Italy), Fax: (+39) 0382-422975
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Abstract

Purified lipase fractions from crude commercial extract of Aspergillus niger lipase (ANL) were selectively immobilized on hydrophobic supports. A significant percentage of esterase activity remains in the supernatant, derived from esterase(s) unable to become adsorbed onto the employed matrices. These residual proteins were covalently immobilized on epoxy-acrylic resin. Immobilized hydrolases were tested in the hydrolysis of acetylated disaccharides in water-cosolvent systems. ANL-Esterase was able to catalyze regioselective deprotection of acetylated β-O-methyl lactoside in C-2 position and β-O-methyl lactosaminide in C-3′ position. The hydrolyzed products, never reported before, can be considered new building blocks for the synthesis of oligosaccharides of biological relevance. Furthermore, preparative hydrolyses were also performed in tert-butanol. This solvent is compatible with ANL-esterase stability and it appears to be a novel and promising approach because of its green status.

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