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

Paul, C. J., Leemhuis, H., Dobruchowska, J. M., Grey, C., Onnby, L., van Leeuwen, S. S., Dijkhuizen, L. & Karlsson, E. N., Sep-2015, In : Applied Microbiology and Biotechnology. 99, 17, p. 7101-7113 13 p.

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  • A GH57 4-alpha-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production

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DOI

  • Catherine J. Paul
  • Hans Leemhuis
  • Justyna M. Dobruchowska
  • Carl Grey
  • Linda Onnby
  • Sander S. van Leeuwen
  • Lubbert Dijkhuizen
  • Eva Nordberg Karlsson

4-alpha-Glucanotransferase (GTase) enzymes (EC 2.4.1.25) modulate the size of alpha-glucans by cleaving and reforming alpha-1,4 glycosidic bonds in alpha-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 alpha-glucan chains from dodecyl-beta-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 A degrees C and an activity half-life of 150 min at 90 A degrees 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.

Original languageEnglish
Pages (from-to)7101-7113
Number of pages13
JournalApplied Microbiology and Biotechnology
Volume99
Issue number17
Publication statusPublished - Sep-2015

    Keywords

  • Amylomaltase, Amylose, Glucan, Glycoside hydrolase, Starch, Alkyl glycoside, MalQ, ALPHA-AMYLASE FAMILY, THERMOCOCCUS-LITORALIS, CYCLODEXTRIN GLYCOSYLTRANSFERASE, TRANSGLYCOSYLATION ACTIVITY, PYROCOCCUS-FURIOSUS, CATALYTIC RESIDUES, ESCHERICHIA-COLI, AMYLOMALTASE, IDENTIFICATION, ENZYMES

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