4-α-Glucanotransferase (GTase) enzymes (EC 126.96.36.199) 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.
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We thank Dr. Thijs Kaper for discussion and Dr. Sonja V. Albers (Molecular Microbiology, University of Groningen) for isolating the genomic DNA of strain DSM8774. Financial support by the EU FP7 research project AMYLOMICS and GreenChem (MISTRA, Sweden) is greatly appreciated. This project is also part-financed by the European Union, European Regional Development Fund and The Netherlands Ministry of Economic Affairs, Agriculture and Innovation, Peaks in the Delta, the Municipality of Groningen, the Province of Groningen, as well as the Dutch Carbohydrate Competence Center (CCC).
Catherine J. Paul and Hans Leemhuis contributed equally to this work.
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Paul, C.J., Leemhuis, H., Dobruchowska, J.M. et al. A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production. Appl Microbiol Biotechnol 99, 7101–7113 (2015). https://doi.org/10.1007/s00253-015-6435-2
- Glycoside hydrolase
- Alkyl glycoside