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Constructing arabinofuranosidases for dual arabinoxylan debranching activity

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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

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en

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Biotechnology and Bioengineering, Volume 115, issue 1, pp. 41-49

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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.

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

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Wang, W, Andric, N, Sarch, C, Silva, B T, Tenkanen, M & Master, E R 2018, 'Constructing arabinofuranosidases for dual arabinoxylan debranching activity', Biotechnology and Bioengineering, vol. 115, no. 1, pp. 41-49. https://doi.org/10.1002/bit.26445

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