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Acceptor specificities of alpha-mannosidases from jack bean and almond, and transmannosylation of branched cyclodextrins.

Authors :
Hara K
Fujita K
Nakano H
Kuwahara N
Tanimoto T
Hashimoto H
Koizumi K
Kitahata S
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.

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