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Transfer action of cyclodextrin glycosyltransferase on starch

Journal Article:

Abstract

The transglycosylation reaction of the cyclodextrin glycosyltransferase from Bacillus megaterium (No. 5 enzyme) and Bacillus macerans (BMA) were examined. No.5 enzyme was more efficient in transglycosylation reaction than BMA in the every acceptor employed in the present study. The order of the efficient acceptors for No. 5 enzyme was maltose (G2), glucose (G1), maltotriose (G3) and sucrose (GF). On the other hand, that found for BMA was G1, G2, GF and G3. The transglycosylation products to glucose formed by the action of No. 5 enzyme on starch were G2, G3, maltotetraose (G4), maltopentaose (G5), maltohexaose (G6) and maltoheptaose (G7) in the order of their quantities, while, in the case of BMA, they were G2, G3, G5, G7 = G4 and G6. The larger transglycosylation products to sucrose formed by the action of No. 5 enzyme on starch were maltosylfructose. On the other hand, that formed by the action of BMA was maltoheptaosylfructose. It was suggested that cyclodextrin glycosyltransferase could transfer the glucosyl residues to an acceptor directly from starch, as well as through cyclodextrin.
Authors:
Kitahata, S; Okada, S [1] 
  1. Osaka City Technical Research Inst. (Japan)
Publication Date:
Nov 01, 1975
Product Type:
Journal Article
Reference Number:
AIX-07-273185; EDB-77-032771
Resource Relation:
Journal Name: Agric. Biol. Chem. (Tokyo); (Japan); Journal Volume: 39:11
Subject:
59 BASIC BIOLOGICAL SCIENCES; TRANSFERASES; BIOCHEMICAL REACTION KINETICS; BACILLUS; CARBON 14 COMPOUNDS; DEXTRIN; GLUCOSE; METABOLISM; SACCHAROSE; STARCH; SUBSTRATES; TRACER TECHNIQUES; ALDEHYDES; BACTERIA; CARBOHYDRATES; DISACCHARIDES; ENZYMES; HEXOSES; ISOTOPE APPLICATIONS; KINETICS; LABELLED COMPOUNDS; MICROORGANISMS; MONOSACCHARIDES; OLIGOSACCHARIDES; ORGANIC COMPOUNDS; POLYSACCHARIDES; REACTION KINETICS; REAGENTS; SACCHARIDES; 550201* - Biochemistry- Tracer Techniques
OSTI ID:
7238682
Country of Origin:
Japan
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: ABCHA
Submitting Site:
INIS
Size:
Pages: 2185-2191
Announcement Date:

Journal Article:

Citation Formats

Kitahata, S, and Okada, S. Transfer action of cyclodextrin glycosyltransferase on starch. Japan: N. p., 1975. Web.
Kitahata, S, & Okada, S. Transfer action of cyclodextrin glycosyltransferase on starch. Japan.
Kitahata, S, and Okada, S. 1975. "Transfer action of cyclodextrin glycosyltransferase on starch." Japan.
@misc{etde_7238682,
title = {Transfer action of cyclodextrin glycosyltransferase on starch}
author = {Kitahata, S, and Okada, S}
abstractNote = {The transglycosylation reaction of the cyclodextrin glycosyltransferase from Bacillus megaterium (No. 5 enzyme) and Bacillus macerans (BMA) were examined. No.5 enzyme was more efficient in transglycosylation reaction than BMA in the every acceptor employed in the present study. The order of the efficient acceptors for No. 5 enzyme was maltose (G2), glucose (G1), maltotriose (G3) and sucrose (GF). On the other hand, that found for BMA was G1, G2, GF and G3. The transglycosylation products to glucose formed by the action of No. 5 enzyme on starch were G2, G3, maltotetraose (G4), maltopentaose (G5), maltohexaose (G6) and maltoheptaose (G7) in the order of their quantities, while, in the case of BMA, they were G2, G3, G5, G7 = G4 and G6. The larger transglycosylation products to sucrose formed by the action of No. 5 enzyme on starch were maltosylfructose. On the other hand, that formed by the action of BMA was maltoheptaosylfructose. It was suggested that cyclodextrin glycosyltransferase could transfer the glucosyl residues to an acceptor directly from starch, as well as through cyclodextrin.}
journal = {Agric. Biol. Chem. (Tokyo); (Japan)}
volume = {39:11}
journal type = {AC}
place = {Japan}
year = {1975}
month = {Nov}
}