Identification and characterization of a novel, cold-adapted D-xylobiose- and D-xylose-releasing endo-β-1,4-xylanase from an antarctic soil bacterium, Duganella sp. PAMC 27433

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Title
Identification and characterization of a novel, cold-adapted D-xylobiose- and D-xylose-releasing endo-β-1,4-xylanase from an antarctic soil bacterium, Duganella sp. PAMC 27433
Author(s)
Do Young KimJonghoon Kim; Y M Lee; J S Lee; D H Shin; B H Ku; Kwang-Hee SonHo-Yong Park
Bibliographic Citation
Biomolecules, vol. 11, no. 5, pp. 680-680
Publication Year
2021
Abstract
Endo-β-1,4-xylanase is a key enzyme in the degradation of β-1,4-d-xylan polysaccharides through hydrolysis. A glycoside hydrolase family 10 (GH10) endo-β-1,4-xylanase (XylR) from Duganella sp. PAMC 27433, an Antarctic soil bacterium, was identified and functionally characterized. The XylR gene (1122-bp) encoded an acidic protein containing a single catalytic GH10 domain that was 86% identical to that of an uncultured bacterium BLR13 endo-β-1,4-xylanase (ACN58881). The recombinant enzyme (rXylR: 42.0 kDa) showed the highest beechwood xylan-degrading activity at pH 5.5 and 40 °C, and displayed 12% of its maximum activity even at 4 °C. rXylR was not only almost completely inhibited by 5 mM N-bromosuccinimide or metal ions (each 1 mM) including Hg2+, Ca2+, or Cu2+ but also significantly suppressed by 1 mM Ni2+, Zn2+, or Fe2+. However, its enzyme activity was upregulated (>1.4-fold) in the presence of 0.5% Triton X-100 or Tween 80. The specific activities of rXylR toward beechwood xylan, birchwood xylan, oat spelts xylan, and p-nitrophenyl-β-d-cellobioside were 274.7, 103.2, 35.6, and 365.1 U/mg, respectively. Enzymatic hydrolysis of birchwood xylan and d-xylooligosaccharides yielded d-xylose and d-xylobiose as the end products. The results of the present study suggest that rXylR is a novel cold-adapted d-xylobiose- and d-xylose-releasing endo-β-1,4-xylanase.
Keyword
Antarctic bacteriumDuganella sp.GH10Cold-adaptedEndo-β-1,4-xylanase
ISSN
2218-273X
Publisher
MDPI
DOI
http://dx.doi.org/10.3390/biom11050680
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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