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

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A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production. / Paul, Catherine; Leemhuis, Hans; Dobruchowska, Justyna M; Grey, Carl; Önnby, Linda; van Leeuwen, Sander S; Dijkhuizen, Lubbert; Nordberg Karlsson, Eva.

I: Applied Microbiology and Biotechnology, Vol. 99, Nr. 17, 2015, s. 7101-7113.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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Paul, Catherine ; Leemhuis, Hans ; Dobruchowska, Justyna M ; Grey, Carl ; Önnby, Linda ; van Leeuwen, Sander S ; Dijkhuizen, Lubbert ; Nordberg Karlsson, Eva. / A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production. I: Applied Microbiology and Biotechnology. 2015 ; Vol. 99, Nr. 17. s. 7101-7113.

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TY - JOUR

T1 - A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production.

AU - Paul, Catherine

AU - Leemhuis, Hans

AU - Dobruchowska, Justyna M

AU - Grey, Carl

AU - Önnby, Linda

AU - van Leeuwen, Sander S

AU - Dijkhuizen, Lubbert

AU - Nordberg Karlsson, Eva

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

U2 - 10.1007/s00253-015-6435-2

DO - 10.1007/s00253-015-6435-2

M3 - Article

C2 - 25693671

VL - 99

SP - 7101

EP - 7113

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 1432-0614

IS - 17

ER -