Complexation of alkyl glycosides with α-cyclodextrin can have drastically different effects on their conversion by glycoside hydrolases.
Rather, Younus LU ; Nordberg Karlsson, Eva LU
and Adlercreutz, Patrick
LU
(2015)
In Journal of Biotechnology
200.
p.52-58
- Abstract
- Substrates present in aggregated forms, such as micelles, are often poorly converted by enzymes. Alkyl glycosides constitute typical examples and the critical micelle concentration (CMC) decreases with increasing length of the alkyl group. In this study, possibilities to hydrolyse alkyl glycosides by glycoside hydrolases were explored, and α-cyclodextrin was used as an agent to form inclusion complexes with the alkyl glycosides, thereby preventing micelle formation. The cyclodextrin complexes were accepted as substrates by the enzymes to variable extent. The β-glucosidases originating from Thermotoga neapolitana (Tn Bgl3B) and from almond were not at all able to hydrolyse alkyl β-glucosides in the presence of 100mM α-cyclodextrin. However,... (More)
- Substrates present in aggregated forms, such as micelles, are often poorly converted by enzymes. Alkyl glycosides constitute typical examples and the critical micelle concentration (CMC) decreases with increasing length of the alkyl group. In this study, possibilities to hydrolyse alkyl glycosides by glycoside hydrolases were explored, and α-cyclodextrin was used as an agent to form inclusion complexes with the alkyl glycosides, thereby preventing micelle formation. The cyclodextrin complexes were accepted as substrates by the enzymes to variable extent. The β-glucosidases originating from Thermotoga neapolitana (Tn Bgl3B) and from almond were not at all able to hydrolyse alkyl β-glucosides in the presence of 100mM α-cyclodextrin. However, Aspergillus niger amyloglucosidase readily accepted the complexes as substrates. In reactions involving decyl and dodecyl maltosides, the presence of 100mM α-cyclodextrin caused an increase in reaction rate in most cases, especially at high substrate concentrations. Surprisingly, the amyloglucosidase-catalyzed hydrolysis of octyl-β-maltoside to glucose and β-octylglucoside was faster in the presence of α-cyclodextrin than without, even at substrate concentrations below CMC. A possible explanation of the observed rate enhancement is that binding sites on the carbohydrate binding domain of amyloglucosidase, known to bind cyclodextrins, help to guide the alkyl glycoside-cyclodextrin complex to the active site, and thereby promote its conversion. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5142904
- author
- Rather, Younus
LU
; Nordberg Karlsson, Eva
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biotechnology
- volume
- 200
- pages
- 52 - 58
- publisher
- Elsevier
- external identifiers
-
- pmid:25711178
- wos:000352017700010
- scopus:84925063721
- pmid:25711178
- ISSN
- 1873-4863
- DOI
- 10.1016/j.jbiotec.2015.02.019
- language
- English
- LU publication?
- yes
- id
- 47754942-f6e7-460d-80a2-9d55796c0168 (old id 5142904)
- date added to LUP
- 2016-04-01 09:58:05
- date last changed
- 2022-04-12 00:41:29
@article{47754942-f6e7-460d-80a2-9d55796c0168,
abstract = {{Substrates present in aggregated forms, such as micelles, are often poorly converted by enzymes. Alkyl glycosides constitute typical examples and the critical micelle concentration (CMC) decreases with increasing length of the alkyl group. In this study, possibilities to hydrolyse alkyl glycosides by glycoside hydrolases were explored, and α-cyclodextrin was used as an agent to form inclusion complexes with the alkyl glycosides, thereby preventing micelle formation. The cyclodextrin complexes were accepted as substrates by the enzymes to variable extent. The β-glucosidases originating from Thermotoga neapolitana (Tn Bgl3B) and from almond were not at all able to hydrolyse alkyl β-glucosides in the presence of 100mM α-cyclodextrin. However, Aspergillus niger amyloglucosidase readily accepted the complexes as substrates. In reactions involving decyl and dodecyl maltosides, the presence of 100mM α-cyclodextrin caused an increase in reaction rate in most cases, especially at high substrate concentrations. Surprisingly, the amyloglucosidase-catalyzed hydrolysis of octyl-β-maltoside to glucose and β-octylglucoside was faster in the presence of α-cyclodextrin than without, even at substrate concentrations below CMC. A possible explanation of the observed rate enhancement is that binding sites on the carbohydrate binding domain of amyloglucosidase, known to bind cyclodextrins, help to guide the alkyl glycoside-cyclodextrin complex to the active site, and thereby promote its conversion.}},
author = {{Rather, Younus and Nordberg Karlsson, Eva and Adlercreutz, Patrick}},
issn = {{1873-4863}},
language = {{eng}},
pages = {{52--58}},
publisher = {{Elsevier}},
series = {{Journal of Biotechnology}},
title = {{Complexation of alkyl glycosides with α-cyclodextrin can have drastically different effects on their conversion by glycoside hydrolases.}},
url = {{http://dx.doi.org/10.1016/j.jbiotec.2015.02.019}},
doi = {{10.1016/j.jbiotec.2015.02.019}},
volume = {{200}},
year = {{2015}},
}