Publication

4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily

Leemhuis, H., Dijkman, W. P., Dobruchowska, J. M., Pijning, T., Grijpstra, P., Kralj, S., Kamerling, J. P., Dijkhuizen, L. & Gerwig, G. J., Jan-2013, In : Applied Microbiology and Biotechnology. 97, 1, p. 181-193 13 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Leemhuis, H., Dijkman, W. P., Dobruchowska, J. M., Pijning, T., Grijpstra, P., Kralj, S., Kamerling, J. P., Dijkhuizen, L., & Gerwig, G. J. (2013). 4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. Applied Microbiology and Biotechnology, 97(1), 181-193. https://doi.org/10.1007/s00253-012-3943-1

Author

Leemhuis, Hans ; Dijkman, Willem P. ; Dobruchowska, Justyna M. ; Pijning, Tjaard ; Grijpstra, Pieter ; Kralj, Slavko ; Kamerling, Johannis P. ; Dijkhuizen, Lubbert ; Gerwig, Gerrit J. / 4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. In: Applied Microbiology and Biotechnology. 2013 ; Vol. 97, No. 1. pp. 181-193.

Harvard

Leemhuis, H, Dijkman, WP, Dobruchowska, JM, Pijning, T, Grijpstra, P, Kralj, S, Kamerling, JP, Dijkhuizen, L & Gerwig, GJ 2013, '4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily', Applied Microbiology and Biotechnology, vol. 97, no. 1, pp. 181-193. https://doi.org/10.1007/s00253-012-3943-1

Standard

4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. / Leemhuis, Hans; Dijkman, Willem P.; Dobruchowska, Justyna M.; Pijning, Tjaard; Grijpstra, Pieter; Kralj, Slavko; Kamerling, Johannis P.; Dijkhuizen, Lubbert; Gerwig, Gerrit J.

In: Applied Microbiology and Biotechnology, Vol. 97, No. 1, 01.2013, p. 181-193.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Leemhuis H, Dijkman WP, Dobruchowska JM, Pijning T, Grijpstra P, Kralj S et al. 4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily. Applied Microbiology and Biotechnology. 2013 Jan;97(1):181-193. https://doi.org/10.1007/s00253-012-3943-1


BibTeX

@article{b9be33e1f5bc4648a16990d654d52a57,
title = "4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily",
abstract = "Family 70 glycoside hydrolase glucansucrase enzymes exclusively occur in lactic acid bacteria and synthesize a wide range of alpha-d-glucan (abbreviated as alpha-glucan) oligo- and polysaccharides. Of the 47 characterized GH70 enzymes, 46 use sucrose as glucose donor. A single GH70 enzyme was recently found to be inactive with sucrose and to utilize maltooligosaccharides [(1 -> 4)-alpha-d-glucooligosaccharides] as glucose donor substrates for alpha-glucan synthesis, acting as a 4,6-alpha-glucanotransferase (4,6-alpha GT) enzyme. Here, we report the characterization of two further GH70 4,6-alpha GT enzymes, i.e., from Lactobacillus reuteri strains DSM 20016 and ML1, which use maltooligosaccharides as glucose donor. Both enzymes cleave alpha 1 -> 4 glycosidic linkages and add the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha 1 -> 6 glycosidic linkages (alpha 1 -> 4 to alpha 1 -> 6 transfer activity). In this way, they convert pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha 1 -> 6 glycosidic bonds (isomalto/maltooligosaccharides). These new alpha-glucan products may provide an exciting type of carbohydrate for the food industry. The results show that 4,6-alpha GTs occur more widespread in family GH70 and can be considered as a GH70 subfamily. Sequence analysis allowed identification of amino acid residues in acceptor substrate binding subsites +1 and +2, differing between GH70 GTF and 4,6-alpha GT enzymes.",
keywords = "alpha-Glucan, Fiber, Glucansucrase, Glycoside hydrolase, 4,6-alpha-Glucanotransferase, Isomaltooligosaccharide, Starch, ALPHA-D-GLUCANS, STRUCTURAL-CHARACTERIZATION, MOLECULAR CHARACTERIZATION, NEISSERIA-POLYSACCHAREA, GLUCONOBACTER-OXYDANS, PRODUCT SPECIFICITY, DEXTRIN DEXTRANASE, REUTERI, ENZYMES, IDENTIFICATION",
author = "Hans Leemhuis and Dijkman, {Willem P.} and Dobruchowska, {Justyna M.} and Tjaard Pijning and Pieter Grijpstra and Slavko Kralj and Kamerling, {Johannis P.} and Lubbert Dijkhuizen and Gerwig, {Gerrit J.}",
year = "2013",
month = jan,
doi = "10.1007/s00253-012-3943-1",
language = "English",
volume = "97",
pages = "181--193",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "SPRINGER",
number = "1",

}

RIS

TY - JOUR

T1 - 4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily

AU - Leemhuis, Hans

AU - Dijkman, Willem P.

AU - Dobruchowska, Justyna M.

AU - Pijning, Tjaard

AU - Grijpstra, Pieter

AU - Kralj, Slavko

AU - Kamerling, Johannis P.

AU - Dijkhuizen, Lubbert

AU - Gerwig, Gerrit J.

PY - 2013/1

Y1 - 2013/1

N2 - Family 70 glycoside hydrolase glucansucrase enzymes exclusively occur in lactic acid bacteria and synthesize a wide range of alpha-d-glucan (abbreviated as alpha-glucan) oligo- and polysaccharides. Of the 47 characterized GH70 enzymes, 46 use sucrose as glucose donor. A single GH70 enzyme was recently found to be inactive with sucrose and to utilize maltooligosaccharides [(1 -> 4)-alpha-d-glucooligosaccharides] as glucose donor substrates for alpha-glucan synthesis, acting as a 4,6-alpha-glucanotransferase (4,6-alpha GT) enzyme. Here, we report the characterization of two further GH70 4,6-alpha GT enzymes, i.e., from Lactobacillus reuteri strains DSM 20016 and ML1, which use maltooligosaccharides as glucose donor. Both enzymes cleave alpha 1 -> 4 glycosidic linkages and add the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha 1 -> 6 glycosidic linkages (alpha 1 -> 4 to alpha 1 -> 6 transfer activity). In this way, they convert pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha 1 -> 6 glycosidic bonds (isomalto/maltooligosaccharides). These new alpha-glucan products may provide an exciting type of carbohydrate for the food industry. The results show that 4,6-alpha GTs occur more widespread in family GH70 and can be considered as a GH70 subfamily. Sequence analysis allowed identification of amino acid residues in acceptor substrate binding subsites +1 and +2, differing between GH70 GTF and 4,6-alpha GT enzymes.

AB - Family 70 glycoside hydrolase glucansucrase enzymes exclusively occur in lactic acid bacteria and synthesize a wide range of alpha-d-glucan (abbreviated as alpha-glucan) oligo- and polysaccharides. Of the 47 characterized GH70 enzymes, 46 use sucrose as glucose donor. A single GH70 enzyme was recently found to be inactive with sucrose and to utilize maltooligosaccharides [(1 -> 4)-alpha-d-glucooligosaccharides] as glucose donor substrates for alpha-glucan synthesis, acting as a 4,6-alpha-glucanotransferase (4,6-alpha GT) enzyme. Here, we report the characterization of two further GH70 4,6-alpha GT enzymes, i.e., from Lactobacillus reuteri strains DSM 20016 and ML1, which use maltooligosaccharides as glucose donor. Both enzymes cleave alpha 1 -> 4 glycosidic linkages and add the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha 1 -> 6 glycosidic linkages (alpha 1 -> 4 to alpha 1 -> 6 transfer activity). In this way, they convert pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha 1 -> 6 glycosidic bonds (isomalto/maltooligosaccharides). These new alpha-glucan products may provide an exciting type of carbohydrate for the food industry. The results show that 4,6-alpha GTs occur more widespread in family GH70 and can be considered as a GH70 subfamily. Sequence analysis allowed identification of amino acid residues in acceptor substrate binding subsites +1 and +2, differing between GH70 GTF and 4,6-alpha GT enzymes.

KW - alpha-Glucan

KW - Fiber

KW - Glucansucrase

KW - Glycoside hydrolase

KW - 4,6-alpha-Glucanotransferase

KW - Isomaltooligosaccharide

KW - Starch

KW - ALPHA-D-GLUCANS

KW - STRUCTURAL-CHARACTERIZATION

KW - MOLECULAR CHARACTERIZATION

KW - NEISSERIA-POLYSACCHAREA

KW - GLUCONOBACTER-OXYDANS

KW - PRODUCT SPECIFICITY

KW - DEXTRIN DEXTRANASE

KW - REUTERI

KW - ENZYMES

KW - IDENTIFICATION

U2 - 10.1007/s00253-012-3943-1

DO - 10.1007/s00253-012-3943-1

M3 - Article

VL - 97

SP - 181

EP - 193

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 1

ER -

ID: 5757195