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Hydrolysis of branched cyclodextrins by a cyclodextrin‐hydrolyzing enzyme from Bacillus sphaericus E‐244
Author(s) -
Oguma Tetsuya,
Kikuchi Mamoru,
Mizusawa Kiyoshi
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81214-s
Subject(s) - cyclodextrin , bacillus sphaericus , chemistry , hydrolysis , alpha (finance) , enzyme , stereochemistry , beta cyclodextrins , beta (programming language) , bacillales , organic chemistry , bacteria , biology , medicine , construct validity , nursing , bacillus subtilis , computer science , patient satisfaction , genetics , programming language
The action of a cyclodextrin‐hydrolyzing enzyme from Bacillus sphaericus E‐244 on branched α‐ and β‐cyclodextrins was investigated. Glucosyl‐α‐cyclodextrin (6‐ O ‐α‐D‐glucosylcyclomaltohexaose) and maltosyl‐α‐cyclodextrin (6‐ O ‐α‐D‐maltosylcyclomaltohexaose) were hydrolyzed to 6 3 ‐ O ‐α‐D‐glucosylmaltohexaose and 6 3 ‐ O ‐α‐D‐maltosylmaltohexaose, respectively. Glucosyl‐β‐cyclodextrin (6‐ O ‐α‐D‐glucosylcyclomaltoheptaose) and maltosyl‐β‐cyclodextrin (6‐ O ‐α‐D‐Maltosylcyclomaltoheptaose) were also transformed mainly to 6 4 ‐ O ‐α‐D‐glucosylmaltoheptaose and 6 4 ‐ O ‐α‐D‐maltosylmaltoheptaose, respectively. These results suggest that the cyclodextrin‐hydrolyzing enzyme cleaves branched α‐ and β‐cyclodextrins at an α‐1,4 linkage which is located furthest from the branching point on the cyclodextrin ring.