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Acceptor specificities of alpha-mannosidases from jack bean and almond, and transmannosylation of branched cyclodextrins.
- Source :
-
Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 1994 Jan; Vol. 58 (1), pp. 60-3. - Publication Year :
- 1994
-
Abstract
- Jack bean alpha-mannosidase had a wide acceptor specificity and could transfer mannosyl residues to various acceptors such as D-fructose, L-arabinose, maltose, lactose, and sucrose. The structures of the transferred products of branched cyclodextrins (CDs) (glucosyl-beta CD, maltosyl-alpha CD, and maltosyl-beta CD) were found to be alpha-D-mannosyl-(1-->6)-alpha-D-glucosyl-(1-->6)-beta CD, alpha-D-mannosyl- (1-->6)-alpha-D-glucosyl-(1-->4)-alpha-D-glucosyl-(1-->6)-alpha CD and alpha-D-mannosyl-(1-->6)-alpha-D-glucosyl-(1-->4)-alpha-D-glucosyl-(1--> 6)- beta CD, respectively. Almond alpha-mannosidase also produced the same transmannosylated products of branched CDs.
- Subjects :
- Carbohydrate Sequence
Chromatography, High Pressure Liquid
Chromatography, Thin Layer
Magnetic Resonance Spectroscopy
Mannosidases isolation & purification
Mannosides metabolism
Methylmannosides
Molecular Sequence Data
Substrate Specificity
alpha-Mannosidase
Cyclodextrins metabolism
Fabaceae enzymology
Mannose metabolism
Mannosidases metabolism
Nuts enzymology
Plants, Medicinal
Subjects
Details
- Language :
- English
- ISSN :
- 0916-8451
- Volume :
- 58
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Bioscience, biotechnology, and biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7764520
- Full Text :
- https://doi.org/10.1271/bbb.58.60