Enzymatic synthesis of novel oligosaccharides from L-sorbose, maltose, andsucrose using kojibiose phosphorylase

Citation
H. Chaen et al., Enzymatic synthesis of novel oligosaccharides from L-sorbose, maltose, andsucrose using kojibiose phosphorylase, J BIOSCI BI, 92(2), 2001, pp. 173-176
Citations number
14
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
13891723 → ACNP
Volume
92
Issue
2
Year of publication
2001
Pages
173 - 176
Database
ISI
SICI code
1389-1723(200108)92:2<173:ESONOF>2.0.ZU;2-Q
Abstract
Glucosyl-L-Sorbose, -maltose, and -sucrose were synthesized using kojibiose phosphorylase (KPase) from Thermoanaerobacter brockii ATCC35047 with beta -D-glucose-1-phosphate (beta -G1P) as a glucosyl donor. One disaccharide an d two trisaccharides thus synthesized were isolated by Toyopearl HW-40S col umn chromatography. The results of KPase digestion, methylation analysis, a nd C-13-NMR studies indicated that these oligosaccharides were alpha -L-glu copyranosyl-(1 -->2)-alpha -L-sorbopyranose, alpha -D-glucopyranosyl-(1 --> 2)-alpha -D-glucopyranosyl-(1 -->4)-D-glucopyranose (4-alpha -D-kojibiosyl- glucose), and alpha -D-glucopyranosyl-(1 -->2)-alpha -D-glucopyranosyl-(1 - ->2)-alpha -D-fructofuranoside, which are all novel oligosaccharides. Gluco syl-L-sorbose was partially hydrolyzed to glucose and L-sorbose by alpha -g lucosidases, while glucosyl-sucrose and glucosyl-maltose were not hydrolyze d by glucoamylase, alpha -glucosidases, or CGTase.