caa a22 4500 605503028 CHVBK 20210128100608.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00253-015-6435-2 doi (NATIONALLICENCE)springer-10.1007/s00253-015-6435-2 A GH57 4-α-glucanotransferase of hyperthermophilic origin with potential for alkyl glycoside production [Elektronische Daten] [Catherine Paul, Hans Leemhuis, Justyna Dobruchowska, Carl Grey, Linda Önnby, Sander van Leeuwen, Lubbert Dijkhuizen, Eva Karlsson] 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 150min 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. Springer-Verlag Berlin Heidelberg, 2015 Amylomaltase nationallicence Amylose nationallicence Glucan nationallicence Glycoside hydrolase nationallicence Starch nationallicence Alkyl glycoside nationallicence MalQ nationallicence Paul Catherine Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut Leemhuis Hans Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut Dobruchowska Justyna Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut Grey Carl Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut Önnby Linda Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut van Leeuwen Sander Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut Dijkhuizen Lubbert Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut Karlsson Eva Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/17(2015-09-01), 7101-7113 0175-7598 99:17<7101 2015 99 253 https://doi.org/10.1007/s00253-015-6435-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-015-6435-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Paul Catherine Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut NATIONALLICENCE 700 1- Leemhuis Hans Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut NATIONALLICENCE 700 1- Dobruchowska Justyna Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut NATIONALLICENCE 700 1- Grey Carl Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut NATIONALLICENCE 700 1- Önnby Linda Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut NATIONALLICENCE 700 1- van Leeuwen Sander Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut NATIONALLICENCE 700 1- Dijkhuizen Lubbert Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), Carbohydrate Competence Center (CCC), University of Groningen, Groningen, Netherlands aut NATIONALLICENCE 700 1- Karlsson Eva Biotechnology, Department of Chemistry, Lund University, Getingevägen 60, 22241, Lund, Sweden aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/17(2015-09-01), 7101-7113 0175-7598 99:17<7101 2015 99 253