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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)
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author
organization
publishing date
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
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
2011-07-27 08:54:05
date last changed
2017-09-03 03:28:11
@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},
  volume       = {155},
  year         = {2011},
}