Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Transglycosylation Activity of Dictyoglomus thermophilum Amylase A
Masahiro NAKAJIMAHiromi IMAMURAHirofumi SHOUNSueharu HORINOUCHITakayoshi WAKAGI
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2004 Volume 68 Issue 11 Pages 2369-2373

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Abstract

Amylase A from Dictyoglomus thermophilum is a thermophilic enzyme and has about 40% identity with 4-α-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. α-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.

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© 2004 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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