๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

An improved method for the preparation of cyclooctaamylose, using starches and the cyclodextrin glycosyltransferase of Klebsiella pneumoniae M 5 al

โœ Scribed by Hans Bender


Publisher
Elsevier Science
Year
1983
Tongue
English
Weight
548 KB
Volume
124
Category
Article
ISSN
0008-6215

No coin nor oath required. For personal study only.

โœฆ Synopsis


Larger amounts (18.7% of total carbohydrate) of cyclooctaamylose (cyclomaltooctaose) were produced from starches by the cyclodextrin glycosyltransferase {(l~4)-a-D-glUCan:[(1~4)-cY-D-glUCOpyranOSyl]tranSferaSC (cyclising), EC 2.4.1.19) of Klebsiellu pneumoniue M 5 al by digestion in 2mmM sodium acetate (pH 6.9) and the addition of bromobenzene after pre-incubation for 7 h. The dependence of the formation of cyclooctaamylose on the concentration of sodium acetate, initial concentration of substrate, and enzyme-substrate ratio has been studied.

A simple method for the preparation of pure cyclooctaamylose has been developed.


๐Ÿ“œ SIMILAR VOLUMES


Branched saccharides formed by the actio
โœ Hans Bender ๐Ÿ“‚ Article ๐Ÿ“… 1991 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 353 KB

Digestion of potato starch with His-modified alpha-cyclodextrin glycosyltransferase from Klebsiella pneumoniae M 5 al yielded branched tetra- to nona-saccharides, as revealed by debranching with pullulanase. Maltose and maltotriose stubs preponderated together with small proportions of D-glucose stu

Studies of the mechanism of the cyclisat
โœ Hans Bender ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 884 KB

The actions of the wildtype and a truncated alpha-cyclodextrin glycosyltransferase from Klebsiella pneumoniae strain M 5 al on malto-oligosaccharides showed no significant differences, and there was marked dependence of the kinetic parameters on the chain lengths of the substrate. The action of the

Cyclodextrin glycosyltransferases from K
โœ Hans Bender ๐Ÿ“‚ Article ๐Ÿ“… 1983 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 621 KB

The analysis of the (1 leads to 4)-alpha-D-glucopyranosyl transfer-products from some linear and cyclic substrates by quantitative h.p.l.c. illuminated the mode of action of the cyclodextrin glycosyltransferases [1 leads to 4)-alpha-D-glucan:[(1 leads to 4)-alpha-D-glucopyranosyl]transferase (cyclis