Hydrolysis of branched cyclodextrins by a cyclodextrin-hydrolyzing enzyme from Bacillus sphaericus E-244.
The action of a cyclodextrin-hydrolyzing enzyme from Bacillus sphaericus E-244 on branched alpha- and beta-cyclodextrins was investigated. Glucosyl-alpha-cyclodextrin (6-O-alpha-D-glucosylcyclomaltohexaose) and maltosyl-alpha-cyclodextrin (6-O-alpha-D-maltosylcyclomaltohexaose) were hydrolyzed to 6(3)-O-alpha-D-glucosylmaltohexaose and 6(3)-O-alpha-D-maltosylmaltohexaose, respectively. Glucosyl-beta-cyclodextrin (6-O-alpha-D-glucosylcyclomaltoheptose) and maltosyl-beta-cyclodextrin (6-O-alpha-D-maltosyclomaltohepatose) were also mainly transformed to 6(4)-O-alpha-D-glucosylmaltoheptaose and 6(4)-O-alpha-D-maltosylmaltoheptaose, respectively. These results suggest that the cyclodextrin-hydrolyzing enzyme cleaves branched alpha- and beta-cyclodextrins at an alpha-1,4 linkage which is located furthest from the branching point on the cyclodextrin ring.
Noda Institute for Scientific Research, Chiba Pref, Japan.
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T
Oguma
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M
Kikuchi
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K
Mizusawa
D001407:Bacillus / Q000201:enzymology; D003505:Cyclodextrins / Q000737:chemistry* / Q000378:metabolism; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D013379:Substrate Specificity
D003505:Cyclodextrins; D005087:Glucan 1,4-alpha-Glucosidase