High-Yielding Enzymatic α-Glucosylation of Pyridoxine by Marine α-Glucosidase from Aplysia fasciata

We recently succeeded in the identification and purification of an interesting marine exo-α-glucosidase (EC 3.2.1.20) from the anaspidean mollusc Aplysia fasciata. The enzyme was characterized by good transglycosylation activity toward different acceptors using maltose as donor. High-yielding enzyma...

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Veröffentlicht in:Marine biotechnology (New York, N.Y.) N.Y.), 2006-09, Vol.8 (5), p.448-452
Hauptverfasser: Tramice, Annabella, Giordano, Assunta, Andreotti, Giuseppina, Mollo, Ernesto, Trincone, Antonio
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container_end_page 452
container_issue 5
container_start_page 448
container_title Marine biotechnology (New York, N.Y.)
container_volume 8
creator Tramice, Annabella
Giordano, Assunta
Andreotti, Giuseppina
Mollo, Ernesto
Trincone, Antonio
description We recently succeeded in the identification and purification of an interesting marine exo-α-glucosidase (EC 3.2.1.20) from the anaspidean mollusc Aplysia fasciata. The enzyme was characterized by good transglycosylation activity toward different acceptors using maltose as donor. High-yielding enzymatic α-glycosylation of pyridoxine using this marine enzyme is reported here; the reaction has been optimized, reaching 80% molar yield of products (pyridoxine monoglucosides 24 g/l; pyridoxine isomaltoside 35 g/l). High selectivity toward the 5′ position is observed for both monoglucoside and disaccharide formation. This is the first report describing the enzymatic production of pyridoxine isomaltoside.
doi_str_mv 10.1007/s10126-005-6144-4
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subjects alpha-Glucosidases - metabolism
Animals
Glycosylation
Molecular Structure
Mollusca - enzymology
Pyridoxine - chemistry
Pyridoxine - metabolism
title High-Yielding Enzymatic α-Glucosylation of Pyridoxine by Marine α-Glucosidase from Aplysia fasciata
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