Publication

Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri

te Poele, E. M., Valk, V., Devlamynck, T., van Leeuwen, S. S. & Dijkhuizen, L., Mar-2017, In : Applied Microbiology and Biotechnology. 101, 11, p. 4495-4505 11 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

te Poele, E. M., Valk, V., Devlamynck, T., van Leeuwen, S. S., & Dijkhuizen, L. (2017). Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri. Applied Microbiology and Biotechnology, 101(11), 4495-4505. https://doi.org/10.1007/s00253-017-8190-z

Author

te Poele, Evelien M ; Valk, Vincent ; Devlamynck, Tim ; van Leeuwen, Sander S ; Dijkhuizen, Lubbert. / Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri. In: Applied Microbiology and Biotechnology. 2017 ; Vol. 101, No. 11. pp. 4495-4505.

Harvard

te Poele, EM, Valk, V, Devlamynck, T, van Leeuwen, SS & Dijkhuizen, L 2017, 'Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri', Applied Microbiology and Biotechnology, vol. 101, no. 11, pp. 4495-4505. https://doi.org/10.1007/s00253-017-8190-z

Standard

Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri. / te Poele, Evelien M; Valk, Vincent; Devlamynck, Tim; van Leeuwen, Sander S; Dijkhuizen, Lubbert.

In: Applied Microbiology and Biotechnology, Vol. 101, No. 11, 03.2017, p. 4495-4505.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

te Poele EM, Valk V, Devlamynck T, van Leeuwen SS, Dijkhuizen L. Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri. Applied Microbiology and Biotechnology. 2017 Mar;101(11):4495-4505. https://doi.org/10.1007/s00253-017-8190-z


BibTeX

@article{2965ea6486104977bc064cd9a48c367c,
title = "Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri",
abstract = "Previously, we have shown that the glucansucrase GtfA-ΔN enzyme of Lactobacillus reuteri 121, incubated with sucrose, efficiently glucosylated catechol and we structurally characterized catechol glucosides with up to five glucosyl units attached (te Poele et al. in Bioconjug Chem 27:937-946, 2016). In the present study, we observed that upon prolonged incubation of GtfA-ΔN with 50 mM catechol and 1000 mM sucrose, all catechol had become completely glucosylated and then started to reappear. Following depletion of sucrose, this glucansucrase GtfA-ΔN used both α-D-Glcp-catechol and α-D-Glcp-(1→4)-α-D-Glcp-catechol as donor substrates and transferred a glucose unit to other catechol glycoside molecules or to sugar oligomers. In the absence of sucrose, GtfA-ΔN used α-D-Glcp-catechol both as donor and acceptor substrate to synthesize catechol glucosides with 2 to 10 glucose units attached and formed gluco-oligosaccharides up to a degree of polymerization of 4. Also two other glucansucrases tested, Gtf180-ΔN from L. reuteri 180 and GtfML1-ΔN from L. reuteri ML1, used α-D-Glcp-catechol and di-glucosyl-catechol as donor/acceptor substrate to synthesize both catechol glucosides and gluco-oligosaccharides. With sucrose as donor substrate, the three glucansucrase enzymes also efficiently glucosylated the phenolic compounds pyrogallol, resorcinol, and ethyl gallate; also these mono-glucosides were used as donor/acceptor substrates.",
keywords = "Glucansucrase, Lactobacillus reuteri, catechol glucosides, acceptor reaction, glucosyl, donor, MOLECULAR CHARACTERIZATION, STRUCTURAL-ANALYSIS, DONOR SUBSTRATE, GLUCAN, DEXTRANSUCRASE, GLUCOSYLTRANSFERASE, SPECIFICITY, SUCROSE, GTFA, REUTERANSUCRASE",
author = "{te Poele}, {Evelien M} and Vincent Valk and Tim Devlamynck and {van Leeuwen}, {Sander S} and Lubbert Dijkhuizen",
year = "2017",
month = "3",
doi = "10.1007/s00253-017-8190-z",
language = "English",
volume = "101",
pages = "4495--4505",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "SPRINGER",
number = "11",

}

RIS

TY - JOUR

T1 - Catechol glucosides act as donor/acceptor substrates of glucansucrase enzymes of Lactobacillus reuteri

AU - te Poele, Evelien M

AU - Valk, Vincent

AU - Devlamynck, Tim

AU - van Leeuwen, Sander S

AU - Dijkhuizen, Lubbert

PY - 2017/3

Y1 - 2017/3

N2 - Previously, we have shown that the glucansucrase GtfA-ΔN enzyme of Lactobacillus reuteri 121, incubated with sucrose, efficiently glucosylated catechol and we structurally characterized catechol glucosides with up to five glucosyl units attached (te Poele et al. in Bioconjug Chem 27:937-946, 2016). In the present study, we observed that upon prolonged incubation of GtfA-ΔN with 50 mM catechol and 1000 mM sucrose, all catechol had become completely glucosylated and then started to reappear. Following depletion of sucrose, this glucansucrase GtfA-ΔN used both α-D-Glcp-catechol and α-D-Glcp-(1→4)-α-D-Glcp-catechol as donor substrates and transferred a glucose unit to other catechol glycoside molecules or to sugar oligomers. In the absence of sucrose, GtfA-ΔN used α-D-Glcp-catechol both as donor and acceptor substrate to synthesize catechol glucosides with 2 to 10 glucose units attached and formed gluco-oligosaccharides up to a degree of polymerization of 4. Also two other glucansucrases tested, Gtf180-ΔN from L. reuteri 180 and GtfML1-ΔN from L. reuteri ML1, used α-D-Glcp-catechol and di-glucosyl-catechol as donor/acceptor substrate to synthesize both catechol glucosides and gluco-oligosaccharides. With sucrose as donor substrate, the three glucansucrase enzymes also efficiently glucosylated the phenolic compounds pyrogallol, resorcinol, and ethyl gallate; also these mono-glucosides were used as donor/acceptor substrates.

AB - Previously, we have shown that the glucansucrase GtfA-ΔN enzyme of Lactobacillus reuteri 121, incubated with sucrose, efficiently glucosylated catechol and we structurally characterized catechol glucosides with up to five glucosyl units attached (te Poele et al. in Bioconjug Chem 27:937-946, 2016). In the present study, we observed that upon prolonged incubation of GtfA-ΔN with 50 mM catechol and 1000 mM sucrose, all catechol had become completely glucosylated and then started to reappear. Following depletion of sucrose, this glucansucrase GtfA-ΔN used both α-D-Glcp-catechol and α-D-Glcp-(1→4)-α-D-Glcp-catechol as donor substrates and transferred a glucose unit to other catechol glycoside molecules or to sugar oligomers. In the absence of sucrose, GtfA-ΔN used α-D-Glcp-catechol both as donor and acceptor substrate to synthesize catechol glucosides with 2 to 10 glucose units attached and formed gluco-oligosaccharides up to a degree of polymerization of 4. Also two other glucansucrases tested, Gtf180-ΔN from L. reuteri 180 and GtfML1-ΔN from L. reuteri ML1, used α-D-Glcp-catechol and di-glucosyl-catechol as donor/acceptor substrate to synthesize both catechol glucosides and gluco-oligosaccharides. With sucrose as donor substrate, the three glucansucrase enzymes also efficiently glucosylated the phenolic compounds pyrogallol, resorcinol, and ethyl gallate; also these mono-glucosides were used as donor/acceptor substrates.

KW - Glucansucrase

KW - Lactobacillus reuteri

KW - catechol glucosides

KW - acceptor reaction

KW - glucosyl

KW - donor

KW - MOLECULAR CHARACTERIZATION

KW - STRUCTURAL-ANALYSIS

KW - DONOR SUBSTRATE

KW - GLUCAN

KW - DEXTRANSUCRASE

KW - GLUCOSYLTRANSFERASE

KW - SPECIFICITY

KW - SUCROSE

KW - GTFA

KW - REUTERANSUCRASE

U2 - 10.1007/s00253-017-8190-z

DO - 10.1007/s00253-017-8190-z

M3 - Article

VL - 101

SP - 4495

EP - 4505

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 11

ER -

ID: 40201308