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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5143366
- author
- 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
- organization
- publishing date
- 2015
- 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
- pmid:25693671
- 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
- 2016-04-01 10:50:12
- date last changed
- 2022-03-12 17:28:32
@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}},
doi = {{10.1007/s00253-015-6435-2}},
volume = {{99}},
year = {{2015}},
}