Constructing arabinofuranosidases for dual arabinoxylan debranching activity

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Constructing arabinofuranosidases for dual arabinoxylan debranching activity. / Wang, Weijun; Andric, Nikola; Sarch, Cody; Silva, Bruno T.; Tenkanen, Maija; Master, Emma R.

In: Biotechnology and Bioengineering, Vol. 115, No. 1, 01.2018, p. 41-49.

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Wang, Weijun ; Andric, Nikola ; Sarch, Cody ; Silva, Bruno T. ; Tenkanen, Maija ; Master, Emma R. / Constructing arabinofuranosidases for dual arabinoxylan debranching activity. In: Biotechnology and Bioengineering. 2018 ; Vol. 115, No. 1. pp. 41-49.

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@article{30c99ffc0a774bb3ad8749ec1ebe3b50,
title = "Constructing arabinofuranosidases for dual arabinoxylan debranching activity",
abstract = "Enzymatic conversion of arabinoxylan requires α-L-arabinofuranosidases able to remove α-L-arabinofuranosyl residues (α-L-Araf) from both mono- and double-substituted D-xylopyranosyl residues (Xylp) in xylan (i.e., AXH-m and AXH-d activity). Herein, SthAbf62A (a family GH62 α-L-arabinofuranosidase with AXH-m activity) and BadAbf43A (a family GH43 α-L-arabinofuranosidase with AXH-d3 activity), were fused to create SthAbf62A_BadAbf43A and BadAbf43A_SthAbf62A. Both fusion enzymes displayed dual AXH-m,d and synergistic activity toward native, highly branched wheat arabinoxylan (WAX). When using a customized arabinoxylan substrate comprising mainly α-(1 → 3)-L-Araf and α-(1 → 2)-L-Araf substituents attached to disubstituted Xylp (d-2,3-WAX), the specific activity of the fusion enzymes was twice that of enzymes added as separate proteins. Moreover, the SthAbf62A_BadAbf43A fusion removed 83{\%} of all α-L-Araf from WAX after a 20 hr treatment. 1H NMR analyses further revealed differences in SthAbf62A_BadAbf43 rate of removal of specific α-L-Araf substituents from WAX, where 9.4 times higher activity was observed toward d-α-(1 → 3)-L-Araf compared to m-α-(1 → 3)-L-Araf positions.",
author = "Weijun Wang and Nikola Andric and Cody Sarch and Silva, {Bruno T.} and Maija Tenkanen and Master, {Emma R.}",
note = "| openaire: EC/H2020/648925/EU//BHIVE",
year = "2018",
month = "1",
doi = "10.1002/bit.26445",
language = "English",
volume = "115",
pages = "41--49",
journal = "Biotechnology and Bioengineering",
issn = "0006-3592",
publisher = "Wiley-Blackwell",
number = "1",

}

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TY - JOUR

T1 - Constructing arabinofuranosidases for dual arabinoxylan debranching activity

AU - Wang, Weijun

AU - Andric, Nikola

AU - Sarch, Cody

AU - Silva, Bruno T.

AU - Tenkanen, Maija

AU - Master, Emma R.

N1 - | openaire: EC/H2020/648925/EU//BHIVE

PY - 2018/1

Y1 - 2018/1

N2 - Enzymatic conversion of arabinoxylan requires α-L-arabinofuranosidases able to remove α-L-arabinofuranosyl residues (α-L-Araf) from both mono- and double-substituted D-xylopyranosyl residues (Xylp) in xylan (i.e., AXH-m and AXH-d activity). Herein, SthAbf62A (a family GH62 α-L-arabinofuranosidase with AXH-m activity) and BadAbf43A (a family GH43 α-L-arabinofuranosidase with AXH-d3 activity), were fused to create SthAbf62A_BadAbf43A and BadAbf43A_SthAbf62A. Both fusion enzymes displayed dual AXH-m,d and synergistic activity toward native, highly branched wheat arabinoxylan (WAX). When using a customized arabinoxylan substrate comprising mainly α-(1 → 3)-L-Araf and α-(1 → 2)-L-Araf substituents attached to disubstituted Xylp (d-2,3-WAX), the specific activity of the fusion enzymes was twice that of enzymes added as separate proteins. Moreover, the SthAbf62A_BadAbf43A fusion removed 83% of all α-L-Araf from WAX after a 20 hr treatment. 1H NMR analyses further revealed differences in SthAbf62A_BadAbf43 rate of removal of specific α-L-Araf substituents from WAX, where 9.4 times higher activity was observed toward d-α-(1 → 3)-L-Araf compared to m-α-(1 → 3)-L-Araf positions.

AB - Enzymatic conversion of arabinoxylan requires α-L-arabinofuranosidases able to remove α-L-arabinofuranosyl residues (α-L-Araf) from both mono- and double-substituted D-xylopyranosyl residues (Xylp) in xylan (i.e., AXH-m and AXH-d activity). Herein, SthAbf62A (a family GH62 α-L-arabinofuranosidase with AXH-m activity) and BadAbf43A (a family GH43 α-L-arabinofuranosidase with AXH-d3 activity), were fused to create SthAbf62A_BadAbf43A and BadAbf43A_SthAbf62A. Both fusion enzymes displayed dual AXH-m,d and synergistic activity toward native, highly branched wheat arabinoxylan (WAX). When using a customized arabinoxylan substrate comprising mainly α-(1 → 3)-L-Araf and α-(1 → 2)-L-Araf substituents attached to disubstituted Xylp (d-2,3-WAX), the specific activity of the fusion enzymes was twice that of enzymes added as separate proteins. Moreover, the SthAbf62A_BadAbf43A fusion removed 83% of all α-L-Araf from WAX after a 20 hr treatment. 1H NMR analyses further revealed differences in SthAbf62A_BadAbf43 rate of removal of specific α-L-Araf substituents from WAX, where 9.4 times higher activity was observed toward d-α-(1 → 3)-L-Araf compared to m-α-(1 → 3)-L-Araf positions.

U2 - 10.1002/bit.26445

DO - 10.1002/bit.26445

M3 - Article

VL - 115

SP - 41

EP - 49

JO - Biotechnology and Bioengineering

JF - Biotechnology and Bioengineering

SN - 0006-3592

IS - 1

ER -

ID: 16195148