Premium
Chemical Synthesis of a Dual Branched Malto‐Decaose: A Potential Substrate for α‐Amylases
Author(s) -
Damager Iben,
Jensen Morten T.,
Olsen Carl E.,
Blennow Andreas,
Møller Birger L.,
Svensson Birte,
Motawia Mohammed S.
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200400449
Subject(s) - tetrasaccharide , oligosaccharide , chemistry , maltose , bacillus licheniformis , amylase , cleavage (geology) , stereochemistry , glycosylation , biochemistry , enzyme , polysaccharide , bacteria , biology , paleontology , bacillus subtilis , fracture (geology) , genetics
A convergent block strategy for general use in efficient synthesis of complex α‐(1→4)‐ and α‐(1→6)‐malto‐oligosaccharides is demonstrated with the first chemical synthesis of a malto‐oligosaccharide, the decasaccharide 6,6′′′′‐bis(α‐maltosyl)‐maltohexaose, with two branch points. Using this chemically defined branched oligosaccharide as a substrate, the cleavage pattern of seven different α‐amylases were investigated. α‐Amylases from human saliva, porcine pancreas, barley α‐amylase 2 and recombinant barley α‐amylase 1 all hydrolysed the decasaccharide selectively. This resulted in a branched hexasaccharide and a branched tetrasaccharide. α‐Amylases from Asperagillus oryzae, Bacillus licheniformis and Bacillus sp. cleaved the decasaccharide at two distinct sites, either producing two branched pentasaccharides, or a branched hexasaccharide and a branched tetrasaccharide. In addition, the enzymes were tested on the single‐branched octasaccharide 6‐α‐maltosyl‐maltohexaose, which was prepared from 6,6′′′′‐bis(α‐maltosyl)‐maltohexaose by treatment with malt limit dextrinase. A similar cleavage pattern to that found for the corresponding linear malto‐oligosaccharide substrate was observed.