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Bioscience Biotechnology and Biochemistry
Article . 2004 . Peer-reviewed
Data sources: Crossref
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Transglycosylation Activity ofDictyoglomus thermophilumAmylase A

Authors: NAKAJIMA, Masahiro; IMAMURA, Hiromi; SHOUN, Hirofumi; HORINOUCHI, Sueharu; WAKAGI, Takayoshi;

Transglycosylation Activity ofDictyoglomus thermophilumAmylase A

Abstract

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.

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Keywords

Glycosylation, Bacteria, cycloamylose, Hydrolysis, Oligosaccharides, Glycogen Debranching Enzyme System, Starch, Amylases, long chain amylose, Escherichia coli, Chromatography, Thin Layer, glucoamylase–resistant molecules, Glucans, Trisaccharides, transglycosylation

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
27
Top 10%
Top 10%
Top 10%
bronze