Acceptor specificity of 4-alpha-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose

Citation
Y. Tachibana et al., Acceptor specificity of 4-alpha-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose, J BIOSCI BI, 90(4), 2000, pp. 406-409
Citations number
15
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
1389-1723 → ACNP
Volume
90
Issue
4
Year of publication
2000
Pages
406 - 409
Database
ISI
SICI code
1389-1723(200010)90:4<406:ASO4FP>2.0.ZU;2-X
Abstract
4-alpha -Glucanotransferase from a hyperthermophilic archaeon Pyrococcus ko dakaraensis KOD1 showed a broad acceptor specificity to various saccharides in an intermolecular transglycosylation reaction. In particular, the enzym e produced large amounts of transfer products of various accepters such as D-glucose, methyl-alpha -D-glucoside, phenyl-a-D-glucoside, and D-xylose. I t is suggested that the requirement for an effective acceptor in the interm olecular transglycosylation reaction catalyzed by this enzyme is the pyrano se structure with the same configurations of the free C2-, C3-, and C4-hydr oxyl groups as D-glucopyranose, like cyclomaltodextrin glucanotransferase ( CGTase). However, the enzyme showed some acceptor specificities unlike thos e of CGTase. Analysis of the action of 4-alpha -glucanotransferase indicate d that the enzyme catalyzes an intramolecular transglycosylation (cyclizati on) reaction of amylose to produce cyclic alpha -1,4-glucan (cycloamylose). The yield of cycloamylose reached 67%, and the degree of polymerization wa s found to range from 16 to above 55.