Characterization of cyclodextrin glycosyltransferases (CGTases) and their application for synthesis of alkyl glycosides with oligomeric head group
Författare
Summary, in English
Cyclodextrin glycosyltransferases (CGTases) from Paenibacillus macerans, Thermoanaerobacter sp. ATCC 53627, Bacillus stearothermophilus and a Carboxydocella sp. (phylogenetically identified from genomic DNA) were characterized with respect to their catalytic activity in different reactions, with emphasis on reactions useful for the elongation of the carbohydrate group of alkyl glycosides. All CGTases had activities between 95 and 115 U/mg in the coupling reaction between a-cyclodextrin (alpha-CD) as glucosyl donor and beta-dodecyl maltoside as glucosyl acceptor, but differed very much in the competing hydrolysis of a-CD. The alpha-CD hydrolysis activity ranged from 0.13 U/mg for P. macerans CGTase to 10.5 U/mg for the Carboxydocella sp. (CspCGT13). Furthermore, the disproportionation activity was much lower for the Paenibacillus CGTase compared to the other CGTases, and consequently this enzyme produced the highest yield of the primary coupling product beta-dodecyl maltooctaoside, which is a valuable surfactant. For production of a polydisperse alkyl glycoside product, disproportionation reactions are useful and the other three CGTases of the current study are efficient catalysts. The newly discovered Carboxydocella sp. (CspCGT13) CGTase has the special feature to produce more of products with even longer carbohydrate groups than the primary coupling product. (C) 2015 Elsevier Ltd. All rights reserved.
Avdelning/ar
Publiceringsår
2015
Språk
Engelska
Sidor
722-728
Publikation/Tidskrift/Serie
Process Biochemistry
Volym
50
Issue
5
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Biocatalysis and Enzyme Technology
Nyckelord
- Cyclodextrin glycosyltransferase
- Disproportionation
- Coupling
- beta-Dodecyl maltoside
- beta-Dodecyl maltooctaoside
- alpha-Cyclodextrin
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1873-3298