Publication

Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655

Meng, X., Gangoiti, J., de Kok, N., van Leeuwen, S. S., Pijning, T. & Dijkhuizen, L., 1-Jul-2018, In : Food Chemistry. 253, p. 236-246 11 p., j.foodchem.2018.01.154.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Meng, X., Gangoiti, J., de Kok, N., van Leeuwen, S. S., Pijning, T., & Dijkhuizen, L. (2018). Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655. Food Chemistry, 253, 236-246. [j.foodchem.2018.01.154]. https://doi.org/10.1016/j.foodchem.2018.01.154

Author

Meng, Xiangfeng ; Gangoiti, Joana ; de Kok, Niels ; van Leeuwen, Sander S ; Pijning, Tjaard ; Dijkhuizen, Lubbert. / Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655. In: Food Chemistry. 2018 ; Vol. 253. pp. 236-246.

Harvard

Meng, X, Gangoiti, J, de Kok, N, van Leeuwen, SS, Pijning, T & Dijkhuizen, L 2018, 'Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655', Food Chemistry, vol. 253, j.foodchem.2018.01.154, pp. 236-246. https://doi.org/10.1016/j.foodchem.2018.01.154

Standard

Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655. / Meng, Xiangfeng; Gangoiti, Joana; de Kok, Niels; van Leeuwen, Sander S; Pijning, Tjaard; Dijkhuizen, Lubbert.

In: Food Chemistry, Vol. 253, j.foodchem.2018.01.154, 01.07.2018, p. 236-246.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Meng X, Gangoiti J, de Kok N, van Leeuwen SS, Pijning T, Dijkhuizen L. Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655. Food Chemistry. 2018 Jul 1;253:236-246. j.foodchem.2018.01.154. https://doi.org/10.1016/j.foodchem.2018.01.154


BibTeX

@article{afe03d0a23dd43a692c81c6c473ccd80,
title = "Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655",
abstract = "Nine GtfB-like 4,6-α-glucanotransferases (4,6-α-GTs) (represented by GtfX of L. aviarius subsp. aviarius DSM 20655) were identified to show distinct characteristics in conserved motifs I-IV. In particular, the {"}fingerprint{"} Tyr in motif III of these nine GtfB-type 4,6-α-GTs was found to be replaced by a Trp. In L. aviarius subsp. aviarius DSM20655, a second GtfB-like protein (GtfY), containing the canonical GtfB Tyr residue in motif III, was located directly upstream of GtfX. Biochemical characterization revealed that both GtfX and GtfY showed GtfB-like 4,6-α-GT activity, cleaving (α1→4) linkages and catalyzing the synthesis of (α1→6) linkages. Nonetheless, they differ in product specificity; GtfY only synthesizes consecutive (α1→6) linkages, yielding linear α-glucan products, but GtfX catalyzes the synthesis of (α1→6) linkages predominantly at branch points (22%) rather than in linear segments (10%). The highly branched α-glucan produced by GtfX from amylose V is resistant to digestion by α-amylase, offering great potential as dietary fibers.",
keywords = "alpha-glucan, 4,6-alpha-Glucanotransferase, Family GH70, Lactic acid bacteria, Glucansucrase, Polysaccharides, LACTIC-ACID BACTERIA, STRUCTURAL-CHARACTERIZATION, MOLECULAR CHARACTERIZATION, GLUCANSUCRASE GTF180, ACTIVE-SITE, REUTERI 121, ENZYMES, GLUCAN, STARCH, GTFB",
author = "Xiangfeng Meng and Joana Gangoiti and {de Kok}, Niels and {van Leeuwen}, {Sander S} and Tjaard Pijning and Lubbert Dijkhuizen",
note = "Copyright {\textcopyright} 2018 The Author(s). Published by Elsevier Ltd.. All rights reserved.",
year = "2018",
month = jul,
day = "1",
doi = "10.1016/j.foodchem.2018.01.154",
language = "English",
volume = "253",
pages = "236--246",
journal = "Food Chemistry",
issn = "1873-7072",
publisher = "ELSEVIER SCI LTD",

}

RIS

TY - JOUR

T1 - Biochemical characterization of two GH70 family 4,6-α-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655

AU - Meng, Xiangfeng

AU - Gangoiti, Joana

AU - de Kok, Niels

AU - van Leeuwen, Sander S

AU - Pijning, Tjaard

AU - Dijkhuizen, Lubbert

N1 - Copyright © 2018 The Author(s). Published by Elsevier Ltd.. All rights reserved.

PY - 2018/7/1

Y1 - 2018/7/1

N2 - Nine GtfB-like 4,6-α-glucanotransferases (4,6-α-GTs) (represented by GtfX of L. aviarius subsp. aviarius DSM 20655) were identified to show distinct characteristics in conserved motifs I-IV. In particular, the "fingerprint" Tyr in motif III of these nine GtfB-type 4,6-α-GTs was found to be replaced by a Trp. In L. aviarius subsp. aviarius DSM20655, a second GtfB-like protein (GtfY), containing the canonical GtfB Tyr residue in motif III, was located directly upstream of GtfX. Biochemical characterization revealed that both GtfX and GtfY showed GtfB-like 4,6-α-GT activity, cleaving (α1→4) linkages and catalyzing the synthesis of (α1→6) linkages. Nonetheless, they differ in product specificity; GtfY only synthesizes consecutive (α1→6) linkages, yielding linear α-glucan products, but GtfX catalyzes the synthesis of (α1→6) linkages predominantly at branch points (22%) rather than in linear segments (10%). The highly branched α-glucan produced by GtfX from amylose V is resistant to digestion by α-amylase, offering great potential as dietary fibers.

AB - Nine GtfB-like 4,6-α-glucanotransferases (4,6-α-GTs) (represented by GtfX of L. aviarius subsp. aviarius DSM 20655) were identified to show distinct characteristics in conserved motifs I-IV. In particular, the "fingerprint" Tyr in motif III of these nine GtfB-type 4,6-α-GTs was found to be replaced by a Trp. In L. aviarius subsp. aviarius DSM20655, a second GtfB-like protein (GtfY), containing the canonical GtfB Tyr residue in motif III, was located directly upstream of GtfX. Biochemical characterization revealed that both GtfX and GtfY showed GtfB-like 4,6-α-GT activity, cleaving (α1→4) linkages and catalyzing the synthesis of (α1→6) linkages. Nonetheless, they differ in product specificity; GtfY only synthesizes consecutive (α1→6) linkages, yielding linear α-glucan products, but GtfX catalyzes the synthesis of (α1→6) linkages predominantly at branch points (22%) rather than in linear segments (10%). The highly branched α-glucan produced by GtfX from amylose V is resistant to digestion by α-amylase, offering great potential as dietary fibers.

KW - alpha-glucan

KW - 4,6-alpha-Glucanotransferase

KW - Family GH70

KW - Lactic acid bacteria

KW - Glucansucrase

KW - Polysaccharides

KW - LACTIC-ACID BACTERIA

KW - STRUCTURAL-CHARACTERIZATION

KW - MOLECULAR CHARACTERIZATION

KW - GLUCANSUCRASE GTF180

KW - ACTIVE-SITE

KW - REUTERI 121

KW - ENZYMES

KW - GLUCAN

KW - STARCH

KW - GTFB

U2 - 10.1016/j.foodchem.2018.01.154

DO - 10.1016/j.foodchem.2018.01.154

M3 - Article

C2 - 29502827

VL - 253

SP - 236

EP - 246

JO - Food Chemistry

JF - Food Chemistry

SN - 1873-7072

M1 - j.foodchem.2018.01.154

ER -

ID: 55322566