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Title 

Novel modular endo-β-1,4-xylanase with transglycosylation activity from Cellulosimicrobium sp. strain HY-13 that is homologous to inverting GH family 6 enzymes

Authors 

Do Young KimS J HamHyo Jeong KimJ KimM H LeeHan-Young ChoD H ShinY H RheeKwang Hee SonHo Yong Park

Publisher 

Elsevier

Issue Date 

2012

Citation 

Bioresource Technology, vol. 107, no. 1, pp. 25-32

Keywords 

Cellulosimicrobium sp. strain HY-13Eisenia fetidaEndo-β-1,4-xylanaseGut bacteriumTransglycosylation activity

Abstract 

The gene (2304-bp) encoding a novel xylanolytic enzyme (XylK2) with a catalytic domain, which is 70% identical to that of Cellulomonas flavigena DSM 20109 GH6 β-1,4-cellobiohydrolase, was identified from an earthworm (Eisenia fetida)-symbiotic bacterium, Cellulosimicrobium sp. strain HY-13. The enzyme consisted of an N-terminal catalytic GH6-like domain, a fibronectin type 3 (Fn3) domain, and a C-terminal carbohydrate-binding module 2 (CBM 2). XylK2ΔFn3-CBM 2 displayed high transferase activity (788.3 IU mg -1) toward p-nitrophenyl (PNP) cellobioside, but did not degrade xylobiose, glucose-based materials, or other PNP-sugar derivatives. Birchwood xylan was degraded by XylK2ΔFn3-CBM 2 to xylobiose (59.2%) and xylotriose (40.8%). The transglycosylation activity of the enzyme, which enabled the formation of xylobiose (33.6%) and xylotriose (66.4%) from the hydrolysis of xylotriose, indicates that it is not an inverting enzyme but a retaining enzyme. The endo-β-1,4-xylanase activity of XylK2ΔFn3-CBM 2 increased significantly by approximately 2.0-fold in the presence of 50 mM xylobiose.

ISSN 

0960-8524

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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