
doi: 10.1271/bbb.68.2369
pmid: 15564678
Amylase A from Dictyoglomus thermophilum is a thermophilic enzyme and has about 40% identity with 4-alpha-glucanotransferase (GTase) from Thermococcus litoralis, and both of these enzymes belong to family 57 glycosyl hydrolase. Since the transglycosylation activity of T. litoralis GTase has been well characterized, the substrate specificity and reaction products of amylase A from D. thermophilum were examined. alpha-1,4 Glucan was produced from maltooligosaccharides, and glucoamylase-resistant molecules (cycloamyloses) were produced from longer chain amylose (average molecular mass 200 kDa). It has been reported that amylase A from D. thermophilum hydrolyzes starch, but in this study it was found that the enzyme was also able to use maltooligosaccharides and long chain amylose as substrate and has transglycosylation activity.
Glycosylation, Bacteria, Hydrolysis, Oligosaccharides, Glycogen Debranching Enzyme System, Starch, Amylases, Escherichia coli, Chromatography, Thin Layer, Glucans, Trisaccharides
Glycosylation, Bacteria, Hydrolysis, Oligosaccharides, Glycogen Debranching Enzyme System, Starch, Amylases, Escherichia coli, Chromatography, Thin Layer, Glucans, Trisaccharides
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