Substrate complexation and aggregation influence the cyclodextrin glycosyltransferase (CGTase) catalyzed synthesis of alkyl glycosides.
Zehentgruber, Daniela LU ; Lundemo, Pontus LU ; Svensson, David LU and Adlercreutz, Patrick LU
(2011)
In Journal of Biotechnology
155.
p.232-235
- Abstract
- Bacillus macerans cyclodextrin glycosyltransferase (CGTase) was used to convert dodecyl-β-maltoside (DDM) to dodecyl-β-maltooctaoside (DDMO) using α-cyclodextrin (α-CD) or starch as glycosyl donors. At 300mM α-CD, varied DDM concentration and 60°C, the reaction obeyed Michaelis-Menten kinetics with a K(m) value of 18mM and a V(max) value of 100U/mg enzyme. However, at 25mM α-CD the reaction rate decreased with increasing DDM concentration (5-50mM), and when the α-CD concentration was varied at fixed DDM concentration an S shaped curve was obtained. The deviations from Michaelis-Menten kinetics were interpreted as being caused by formation of inclusion complexes between α-CD and DDM and by micellation of DDM. To achieve a high... (More)
- Bacillus macerans cyclodextrin glycosyltransferase (CGTase) was used to convert dodecyl-β-maltoside (DDM) to dodecyl-β-maltooctaoside (DDMO) using α-cyclodextrin (α-CD) or starch as glycosyl donors. At 300mM α-CD, varied DDM concentration and 60°C, the reaction obeyed Michaelis-Menten kinetics with a K(m) value of 18mM and a V(max) value of 100U/mg enzyme. However, at 25mM α-CD the reaction rate decreased with increasing DDM concentration (5-50mM), and when the α-CD concentration was varied at fixed DDM concentration an S shaped curve was obtained. The deviations from Michaelis-Menten kinetics were interpreted as being caused by formation of inclusion complexes between α-CD and DDM and by micellation of DDM. To achieve a high reaction rate, a high concentration of free α-CD is necessary, since α-CD in the form of a complex has low reactivity. When starch is used as glycosyl donor in the CGTase catalyzed alkyl glycoside elongation reaction, it is thus important to choose reaction conditions under which the cyclization of starch to α-CD is efficient. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2059113
- author
- Zehentgruber, Daniela
LU
; Lundemo, Pontus
LU
; Svensson, David
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biotechnology
- volume
- 155
- pages
- 232 - 235
- publisher
- Elsevier
- external identifiers
-
- wos:000293777800014
- pmid:21723346
- scopus:80051472340
- pmid:21723346
- ISSN
- 1873-4863
- DOI
- 10.1016/j.jbiotec.2011.06.011
- language
- English
- LU publication?
- yes
- id
- e57293a9-c75e-45ab-9f05-278d9f8291d5 (old id 2059113)
- date added to LUP
- 2016-04-01 10:55:34
- date last changed
- 2022-01-26 03:45:59
@article{e57293a9-c75e-45ab-9f05-278d9f8291d5,
abstract = {{Bacillus macerans cyclodextrin glycosyltransferase (CGTase) was used to convert dodecyl-β-maltoside (DDM) to dodecyl-β-maltooctaoside (DDMO) using α-cyclodextrin (α-CD) or starch as glycosyl donors. At 300mM α-CD, varied DDM concentration and 60°C, the reaction obeyed Michaelis-Menten kinetics with a K(m) value of 18mM and a V(max) value of 100U/mg enzyme. However, at 25mM α-CD the reaction rate decreased with increasing DDM concentration (5-50mM), and when the α-CD concentration was varied at fixed DDM concentration an S shaped curve was obtained. The deviations from Michaelis-Menten kinetics were interpreted as being caused by formation of inclusion complexes between α-CD and DDM and by micellation of DDM. To achieve a high reaction rate, a high concentration of free α-CD is necessary, since α-CD in the form of a complex has low reactivity. When starch is used as glycosyl donor in the CGTase catalyzed alkyl glycoside elongation reaction, it is thus important to choose reaction conditions under which the cyclization of starch to α-CD is efficient.}},
author = {{Zehentgruber, Daniela and Lundemo, Pontus and Svensson, David and Adlercreutz, Patrick}},
issn = {{1873-4863}},
language = {{eng}},
pages = {{232--235}},
publisher = {{Elsevier}},
series = {{Journal of Biotechnology}},
title = {{Substrate complexation and aggregation influence the cyclodextrin glycosyltransferase (CGTase) catalyzed synthesis of alkyl glycosides.}},
url = {{http://dx.doi.org/10.1016/j.jbiotec.2011.06.011}},
doi = {{10.1016/j.jbiotec.2011.06.011}},
volume = {{155}},
year = {{2011}},
}