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A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella.

Gulshan Kazi, Zubaida LU ; Lundemo, Pontus LU ; Fridjonsson, Olafur H; Hreggvidson, Gudmundur O; Adlercreutz, Patrick LU and Nordberg Karlsson, Eva LU (2015) In Glycobiology 25(5). p.514-523
Abstract
Cyclodextrin glucanotransferases (CGTases; EC 2.4.1.19) have mainly been characterized for their ability to produce cyclodextrins (CDs) from starch in an intramolecular transglycosylation reaction (cyclization). However, this class of enzymes can also catalyze intermolecular transglycosylation via disproportionation or coupling reactions onto a wide array of acceptors and could therefore be valuable as a tool for glycosylation. In this paper, we report the gene isolation, via the CODEHOP-strategy, expression and characterization of a novel CGTase (CspCGT13) from a Carboxydocella sp. This enzyme is the first glycoside hydrolase isolated from the genus, indicating starch degradation via cyclodextrin production in the Carboxydocella strain.... (More)
Cyclodextrin glucanotransferases (CGTases; EC 2.4.1.19) have mainly been characterized for their ability to produce cyclodextrins (CDs) from starch in an intramolecular transglycosylation reaction (cyclization). However, this class of enzymes can also catalyze intermolecular transglycosylation via disproportionation or coupling reactions onto a wide array of acceptors and could therefore be valuable as a tool for glycosylation. In this paper, we report the gene isolation, via the CODEHOP-strategy, expression and characterization of a novel CGTase (CspCGT13) from a Carboxydocella sp. This enzyme is the first glycoside hydrolase isolated from the genus, indicating starch degradation via cyclodextrin production in the Carboxydocella strain. The fundamental reactivities of this novel CGTase are characterized and compared to two commercial CGTases, assayed under identical condition, in order to facilitate interpretation of the results. The comparison showed that the enzyme, CspCGT13, displayed high coupling activity using γ-CD as donor, despite preferentially forming α and β-CD in the cyclization reaction using wheat starch as substrate. Comparison of subsite conservation within previously characterized CGTases showed significant sequence variation in subsite -3 and -7, which may be important for the coupling activity. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Glycobiology
volume
25
issue
5
pages
514 - 523
publisher
Oxford University Press
external identifiers
  • pmid:25512632
  • wos:000353902000005
  • scopus:84942243886
ISSN
1460-2423
DOI
10.1093/glycob/cwu182
language
English
LU publication?
yes
id
76ea4546-69ad-4007-8041-e6a31487a3bf (old id 4908183)
date added to LUP
2015-01-19 17:32:46
date last changed
2017-07-23 03:21:01
@article{76ea4546-69ad-4007-8041-e6a31487a3bf,
  abstract     = {Cyclodextrin glucanotransferases (CGTases; EC 2.4.1.19) have mainly been characterized for their ability to produce cyclodextrins (CDs) from starch in an intramolecular transglycosylation reaction (cyclization). However, this class of enzymes can also catalyze intermolecular transglycosylation via disproportionation or coupling reactions onto a wide array of acceptors and could therefore be valuable as a tool for glycosylation. In this paper, we report the gene isolation, via the CODEHOP-strategy, expression and characterization of a novel CGTase (CspCGT13) from a Carboxydocella sp. This enzyme is the first glycoside hydrolase isolated from the genus, indicating starch degradation via cyclodextrin production in the Carboxydocella strain. The fundamental reactivities of this novel CGTase are characterized and compared to two commercial CGTases, assayed under identical condition, in order to facilitate interpretation of the results. The comparison showed that the enzyme, CspCGT13, displayed high coupling activity using γ-CD as donor, despite preferentially forming α and β-CD in the cyclization reaction using wheat starch as substrate. Comparison of subsite conservation within previously characterized CGTases showed significant sequence variation in subsite -3 and -7, which may be important for the coupling activity.},
  author       = {Gulshan Kazi, Zubaida and Lundemo, Pontus and Fridjonsson, Olafur H and Hreggvidson, Gudmundur O and Adlercreutz, Patrick and Nordberg Karlsson, Eva},
  issn         = {1460-2423},
  language     = {eng},
  number       = {5},
  pages        = {514--523},
  publisher    = {Oxford University Press},
  series       = {Glycobiology},
  title        = {A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella.},
  url          = {http://dx.doi.org/10.1093/glycob/cwu182},
  volume       = {25},
  year         = {2015},
}