Publication

Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose

Gangoiti, J., Pijning, T. & Dijkhuizen, L., Feb-2018, In : Biotechnology Advances. 36, p. 196-207 12 p.

Research output: Contribution to journalReview articleAcademicpeer-review

APA

Gangoiti, J., Pijning, T., & Dijkhuizen, L. (2018). Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose. Biotechnology Advances, 36, 196-207. https://doi.org/10.1016/j.biotechadv.2017.11.001

Author

Gangoiti, Joana ; Pijning, Tjaard ; Dijkhuizen, Lubbert. / Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose. In: Biotechnology Advances. 2018 ; Vol. 36. pp. 196-207.

Harvard

Gangoiti, J, Pijning, T & Dijkhuizen, L 2018, 'Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose', Biotechnology Advances, vol. 36, pp. 196-207. https://doi.org/10.1016/j.biotechadv.2017.11.001

Standard

Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose. / Gangoiti, Joana; Pijning, Tjaard; Dijkhuizen, Lubbert.

In: Biotechnology Advances, Vol. 36, 02.2018, p. 196-207.

Research output: Contribution to journalReview articleAcademicpeer-review

Vancouver

Gangoiti J, Pijning T, Dijkhuizen L. Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose. Biotechnology Advances. 2018 Feb;36:196-207. https://doi.org/10.1016/j.biotechadv.2017.11.001


BibTeX

@article{9cdf61147a5f4e1eb07711b42c8e48f1,
title = "Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose",
abstract = "Transglucosidases belonging to the glycoside hydrolase (GH) family 70 are promising enzymatic tools for the synthesis of α-glucans with defined structures from renewable sucrose and starch substrates. Depending on the GH70 enzyme specificity, α-glucans with different structures and physicochemical properties are produced, which have found diverse (potential) commercial applications, e.g. in food, health and as biomaterials. Originally, the GH70 family was established only for glucansucrase enzymes of lactic acid bacteria that catalyze the synthesis of α-glucan polymers from sucrose. In recent years, we have identified 3 novel subfamilies of GH70 enzymes (designated GtfB, GtfC and GtfD), inactive on sucrose but converting starch/maltodextrin substrates into novel α-glucans. These novel starch-acting enzymes considerably enlarge the panel of α-glucans that can be produced. They also represent very interesting evolutionary intermediates between sucrose-acting GH70 glucansucrases and starch-acting GH13 α-amylases. Here we provide an overview of the repertoire of GH70 enzymes currently available with focus on these novel starch-acting GH70 enzymes and their biotechnological potential. Moreover, we discuss key developments in the understanding of structure-function relationships of GH70 enzymes in the light of available three-dimensional structure structures, and the protein engineering strategies that were recently applied to expand their natural product specificities.",
keywords = "GH70, Glucansucrase, Glucanotransferase, alpha-glucan, lactic acid bacteria, structure-function, 4,6-ALPHA-GLUCANOTRANSFERASE ENZYMES, BRANCHING SUCRASE, LACTOBACILLUS-REUTERI 180, MESENTEROIDES NRRL B-1299, LACTIC-ACID BACTERIA, STREPTOCOCCUS-MUTANS GLUCOSYLTRANSFERASES, 2 CATALYTIC DOMAINS, LEUCONOSTOC-MESENTEROIDES, MOLECULAR CHARACTERIZATION, STRUCTURAL-ANALYSIS",
author = "Joana Gangoiti and Tjaard Pijning and Lubbert Dijkhuizen",
note = "Copyright {\textcopyright} 2017. Published by Elsevier Inc.",
year = "2018",
month = feb,
doi = "10.1016/j.biotechadv.2017.11.001",
language = "English",
volume = "36",
pages = "196--207",
journal = "Biotechnology Advances",
issn = "0734-9750",

}

RIS

TY - JOUR

T1 - Biotechnological potential of novel glycoside hydrolase family 70 enzymes synthesizing α-glucans from starch and sucrose

AU - Gangoiti, Joana

AU - Pijning, Tjaard

AU - Dijkhuizen, Lubbert

N1 - Copyright © 2017. Published by Elsevier Inc.

PY - 2018/2

Y1 - 2018/2

N2 - Transglucosidases belonging to the glycoside hydrolase (GH) family 70 are promising enzymatic tools for the synthesis of α-glucans with defined structures from renewable sucrose and starch substrates. Depending on the GH70 enzyme specificity, α-glucans with different structures and physicochemical properties are produced, which have found diverse (potential) commercial applications, e.g. in food, health and as biomaterials. Originally, the GH70 family was established only for glucansucrase enzymes of lactic acid bacteria that catalyze the synthesis of α-glucan polymers from sucrose. In recent years, we have identified 3 novel subfamilies of GH70 enzymes (designated GtfB, GtfC and GtfD), inactive on sucrose but converting starch/maltodextrin substrates into novel α-glucans. These novel starch-acting enzymes considerably enlarge the panel of α-glucans that can be produced. They also represent very interesting evolutionary intermediates between sucrose-acting GH70 glucansucrases and starch-acting GH13 α-amylases. Here we provide an overview of the repertoire of GH70 enzymes currently available with focus on these novel starch-acting GH70 enzymes and their biotechnological potential. Moreover, we discuss key developments in the understanding of structure-function relationships of GH70 enzymes in the light of available three-dimensional structure structures, and the protein engineering strategies that were recently applied to expand their natural product specificities.

AB - Transglucosidases belonging to the glycoside hydrolase (GH) family 70 are promising enzymatic tools for the synthesis of α-glucans with defined structures from renewable sucrose and starch substrates. Depending on the GH70 enzyme specificity, α-glucans with different structures and physicochemical properties are produced, which have found diverse (potential) commercial applications, e.g. in food, health and as biomaterials. Originally, the GH70 family was established only for glucansucrase enzymes of lactic acid bacteria that catalyze the synthesis of α-glucan polymers from sucrose. In recent years, we have identified 3 novel subfamilies of GH70 enzymes (designated GtfB, GtfC and GtfD), inactive on sucrose but converting starch/maltodextrin substrates into novel α-glucans. These novel starch-acting enzymes considerably enlarge the panel of α-glucans that can be produced. They also represent very interesting evolutionary intermediates between sucrose-acting GH70 glucansucrases and starch-acting GH13 α-amylases. Here we provide an overview of the repertoire of GH70 enzymes currently available with focus on these novel starch-acting GH70 enzymes and their biotechnological potential. Moreover, we discuss key developments in the understanding of structure-function relationships of GH70 enzymes in the light of available three-dimensional structure structures, and the protein engineering strategies that were recently applied to expand their natural product specificities.

KW - GH70

KW - Glucansucrase

KW - Glucanotransferase

KW - alpha-glucan

KW - lactic acid bacteria

KW - structure-function

KW - 4,6-ALPHA-GLUCANOTRANSFERASE ENZYMES

KW - BRANCHING SUCRASE

KW - LACTOBACILLUS-REUTERI 180

KW - MESENTEROIDES NRRL B-1299

KW - LACTIC-ACID BACTERIA

KW - STREPTOCOCCUS-MUTANS GLUCOSYLTRANSFERASES

KW - 2 CATALYTIC DOMAINS

KW - LEUCONOSTOC-MESENTEROIDES

KW - MOLECULAR CHARACTERIZATION

KW - STRUCTURAL-ANALYSIS

U2 - 10.1016/j.biotechadv.2017.11.001

DO - 10.1016/j.biotechadv.2017.11.001

M3 - Review article

C2 - 29133008

VL - 36

SP - 196

EP - 207

JO - Biotechnology Advances

JF - Biotechnology Advances

SN - 0734-9750

ER -

ID: 50186875