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A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production.

Paul, Catherine LU ; Leemhuis, Hans; Dobruchowska, Justyna M; Grey, Carl LU ; Önnby, Linda LU ; van Leeuwen, Sander S; Dijkhuizen, Lubbert and Nordberg Karlsson, Eva LU (2015) In Applied Microbiology and Biotechnology 99(17). p.7101-7113
Abstract
4-α-Glucanotransferase (GTase) enzymes (EC 2.4.1.25) modulate the size of α-glucans by cleaving and reforming α-1,4 glycosidic bonds in α-glucans, an essential process in starch and glycogen metabolism in plants and microorganisms. The glycoside hydrolase family 57 enzyme (GTase57) studied in the current work catalyzes both disproportionation and cyclization reactions. Amylose was converted into cyclic amylose (with a minimum size of 17 glucose monomers) as well as to a spectrum of maltodextrins, but in contrast to glycoside hydrolase family 13 cyclodextrin glucanotransferases (CGTases), no production of cyclodextrins (C6-C8) was observed. GTase57 also effectively produced alkyl-glycosides with long α-glucan chains from... (More)
4-α-Glucanotransferase (GTase) enzymes (EC 2.4.1.25) modulate the size of α-glucans by cleaving and reforming α-1,4 glycosidic bonds in α-glucans, an essential process in starch and glycogen metabolism in plants and microorganisms. The glycoside hydrolase family 57 enzyme (GTase57) studied in the current work catalyzes both disproportionation and cyclization reactions. Amylose was converted into cyclic amylose (with a minimum size of 17 glucose monomers) as well as to a spectrum of maltodextrins, but in contrast to glycoside hydrolase family 13 cyclodextrin glucanotransferases (CGTases), no production of cyclodextrins (C6-C8) was observed. GTase57 also effectively produced alkyl-glycosides with long α-glucan chains from dodecyl-β-D-maltoside and starch, demonstrating the potential of the enzyme to produce novel variants of surfactants. Importantly, the GTase57 has excellent thermostability with a maximal activity at 95 °C and an activity half-life of 150 min at 90 °C which is highly advantageous in this manufacturing process suggesting that enzymes from this relatively uncharacterized family, GH57, can be powerful biocatalysts for the production of large head group glucosides from soluble starch. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Applied Microbiology and Biotechnology
volume
99
issue
17
pages
7101 - 7113
publisher
Springer
external identifiers
  • pmid:25693671
  • wos:000359739600013
  • scopus:84939252878
ISSN
1432-0614
DOI
10.1007/s00253-015-6435-2
language
English
LU publication?
yes
id
ec23a86f-ba0a-4820-8564-0c973fea1f65 (old id 5143366)
date added to LUP
2015-03-09 17:06:40
date last changed
2017-01-01 03:56:21
@article{ec23a86f-ba0a-4820-8564-0c973fea1f65,
  abstract     = {4-α-Glucanotransferase (GTase) enzymes (EC 2.4.1.25) modulate the size of α-glucans by cleaving and reforming α-1,4 glycosidic bonds in α-glucans, an essential process in starch and glycogen metabolism in plants and microorganisms. The glycoside hydrolase family 57 enzyme (GTase57) studied in the current work catalyzes both disproportionation and cyclization reactions. Amylose was converted into cyclic amylose (with a minimum size of 17 glucose monomers) as well as to a spectrum of maltodextrins, but in contrast to glycoside hydrolase family 13 cyclodextrin glucanotransferases (CGTases), no production of cyclodextrins (C6-C8) was observed. GTase57 also effectively produced alkyl-glycosides with long α-glucan chains from dodecyl-β-D-maltoside and starch, demonstrating the potential of the enzyme to produce novel variants of surfactants. Importantly, the GTase57 has excellent thermostability with a maximal activity at 95 °C and an activity half-life of 150 min at 90 °C which is highly advantageous in this manufacturing process suggesting that enzymes from this relatively uncharacterized family, GH57, can be powerful biocatalysts for the production of large head group glucosides from soluble starch.},
  author       = {Paul, Catherine and Leemhuis, Hans and Dobruchowska, Justyna M and Grey, Carl and Önnby, Linda and van Leeuwen, Sander S and Dijkhuizen, Lubbert and Nordberg Karlsson, Eva},
  issn         = {1432-0614},
  language     = {eng},
  number       = {17},
  pages        = {7101--7113},
  publisher    = {Springer},
  series       = {Applied Microbiology and Biotechnology},
  title        = {A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production.},
  url          = {http://dx.doi.org/10.1007/s00253-015-6435-2},
  volume       = {99},
  year         = {2015},
}