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Chemoenzymatic synthesis of6 ω-S- α- d-glucopyranosyl-6 ω-thiomaltooligosaccharides: their binding toAspergillus nigerglucoamylase G1 and its starch-binding domain

Authors
Journal
Carbohydrate Research
0008-6215
Publisher
Elsevier
Publication Date
Volume
277
Issue
2
Identifiers
DOI: 10.1016/0008-6215(95)00221-e
Keywords
  • Enzymatic Synthesis
  • Cyclodextrin Glucosyltransferase
  • Glucoamylase
  • 6-Deoxy-6-Iodo-β-Cd
  • Modified Maltodextrins
  • Thiomaltodextrins

Abstract

Abstract A coupling reaction of cyclodextrin glucosyltransferase (CGTase) with glucose and 6-deoxy-6-iodo-cyclomaltoheptaose ( 1), in the presence of glucoamylase, followed by acetylation, led to a convenient synthesis of acetylated 6 III-deoxy-6 III-iodo-maltotriose ( 2) and 6 IV-deoxy-6 IV-iodo-maltotetraose ( 3). Nucleophilic displacement of the iodine atom of these protected maltotriose and maltotetraose analogs by the activated form of 2,3,4,6-tetra-O- acetyl-1-S- acetyl-1-thio-α- d-glucose ( 4) afforded peracetylated 6 III -S- α- d-glucopyranosyl-6 III-thiomaltotriose ( 5) and 6 IV -S- α- d-glucopyranosyl-6 IV-thiomaltotetraose ( 6) in high yield. The interaction of OH-free tetra- and penta-saccharides ( 7 and 8) with both glucoamylase G1 from Aspergillus niger as well as its isolated starch-binding domain fragment were studied by UV difference spectroscopy. It was found that the starch-binding domain has higher affinity for 7 and 8 than for maltotetraose and maltopentaose.

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