Abstract
Cyclomaltodextrinases (CDases) belong to Glycoside Hydrolases
(GH) family 13, which show versatile hydrolyzing
and/or transglycosylation activity against cyclodextrin (CD),
starch, and pullulan. Especially, some CDases have been reported
to hydrolyze acarbose, a potent α-glucosidase inhibitor,
and transfer the resulting acarviosine-glucose to various
acceptors. In this study, a novel CDase (LPCD) gene was
cloned from Lactobacillus plantarum WCFS1, which encodes
574 amino acids (64.6 kDa) and shares less than 44% of identities
with the known CDase-family enzymes. Recombinant
LPCD with C-terminal six-histidines was produced and purified
from Escherichia coli. It showed the highest activity
on β-CD at 45°C and pH 5.0, respectively. Gel permeation
chromatography analysis revealed that LPCD exists as a dodecameric
form (~826 kDa). Its hydrolyzing activity on β-
CD is almost same as that on starch, whereas it can hardly
attack pullulan. Most interestingly, LPCD catalyzed the unique
modes of action in acarbose hydrolysis to produce maltose
and acarviosine, as well as to glucose and acarviosineglucose.
Citations
Citations to this article as recorded by

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