alpha-Amylase-catalysed synthesis of alkyl glycosides
Svensson, Julia LU ; Svensson, David LU and Adlercreutz, Patrick LU
(2005)
In Journal of Molecular Catalysis B: Enzymatic
37(1-6).
p.84-87
- Abstract
- Alkyl glycosides were synthesised from starch and alcohols using Aspergillus oryzae a-amylase as catalyst. In the degradation of starch by a-amylase, the alcohols competed with water as glycosyl acceptors. In the reaction with methanol, methyl maltoside and methyl maltotrioside were the main alcoholysis products. Conversion of 45 g/1 starch in 30% methanol resulted in a product mixture containing 26 mM maltooligosaccharides and 3.6 mM methyl glycosides. With ethanol, propanol and butanol, alkyl maltosides and alkyl maltotetraosides were detected, and with benzyl alcohol, benzyl glycosides having two, three or five glucose units were formed. No alcoholysis reaction occurred with hexanol or octanol. In conclusion, alpha-amylase is promising... (More)
- Alkyl glycosides were synthesised from starch and alcohols using Aspergillus oryzae a-amylase as catalyst. In the degradation of starch by a-amylase, the alcohols competed with water as glycosyl acceptors. In the reaction with methanol, methyl maltoside and methyl maltotrioside were the main alcoholysis products. Conversion of 45 g/1 starch in 30% methanol resulted in a product mixture containing 26 mM maltooligosaccharides and 3.6 mM methyl glycosides. With ethanol, propanol and butanol, alkyl maltosides and alkyl maltotetraosides were detected, and with benzyl alcohol, benzyl glycosides having two, three or five glucose units were formed. No alcoholysis reaction occurred with hexanol or octanol. In conclusion, alpha-amylase is promising for the one-step synthesis of alkyl glycosides having more than one monosaccharide unit, which are difficult to synthesise in other ways. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/210737
- author
- Svensson, Julia
LU
; Svensson, David
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- biodegradable surfactant, alpha-amylase, alkyl glycoside, biosurfactant, alcoholysis
- in
- Journal of Molecular Catalysis B: Enzymatic
- volume
- 37
- issue
- 1-6
- pages
- 84 - 87
- publisher
- Elsevier
- external identifiers
-
- wos:000234026100013
- scopus:27944490764
- ISSN
- 1873-3158
- DOI
- 10.1016/j.molcatb.2005.09.009
- language
- English
- LU publication?
- yes
- id
- 498e0b6c-61f7-427b-ad5f-a509f57d0429 (old id 210737)
- date added to LUP
- 2016-04-01 11:38:47
- date last changed
- 2022-04-20 19:41:21
@article{498e0b6c-61f7-427b-ad5f-a509f57d0429,
abstract = {{Alkyl glycosides were synthesised from starch and alcohols using Aspergillus oryzae a-amylase as catalyst. In the degradation of starch by a-amylase, the alcohols competed with water as glycosyl acceptors. In the reaction with methanol, methyl maltoside and methyl maltotrioside were the main alcoholysis products. Conversion of 45 g/1 starch in 30% methanol resulted in a product mixture containing 26 mM maltooligosaccharides and 3.6 mM methyl glycosides. With ethanol, propanol and butanol, alkyl maltosides and alkyl maltotetraosides were detected, and with benzyl alcohol, benzyl glycosides having two, three or five glucose units were formed. No alcoholysis reaction occurred with hexanol or octanol. In conclusion, alpha-amylase is promising for the one-step synthesis of alkyl glycosides having more than one monosaccharide unit, which are difficult to synthesise in other ways.}},
author = {{Svensson, Julia and Svensson, David and Adlercreutz, Patrick}},
issn = {{1873-3158}},
keywords = {{biodegradable surfactant; alpha-amylase; alkyl glycoside; biosurfactant; alcoholysis}},
language = {{eng}},
number = {{1-6}},
pages = {{84--87}},
publisher = {{Elsevier}},
series = {{Journal of Molecular Catalysis B: Enzymatic}},
title = {{alpha-Amylase-catalysed synthesis of alkyl glycosides}},
url = {{http://dx.doi.org/10.1016/j.molcatb.2005.09.009}},
doi = {{10.1016/j.molcatb.2005.09.009}},
volume = {{37}},
year = {{2005}},
}