A CGTase with high coupling activity using γ-cyclodextrin isolated from a novel strain clustering under the genus Carboxydocella.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4908183
- author
- Gulshan Kazi, Zubaida LU ; Lundemo, Pontus LU ; Fridjonsson, Olafur H ; Hreggvidson, Gudmundur O ; Adlercreutz, Patrick LU and Nordberg Karlsson, Eva LU
- organization
- publishing date
- 2015
- 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
- pmid:25512632
- 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
- 2016-04-01 10:40:43
- date last changed
- 2024-02-21 22:13:41
@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}}, doi = {{10.1093/glycob/cwu182}}, volume = {{25}}, year = {{2015}}, }