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Title 

Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: Biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues

Authors 

Do Young KimM K HanHyun Woo OhKyung Sook BaeTae Sook JeongSung Uk KimD H ShinI H KimY H RheeKwang Hee SonHo Yong Park

Publisher 

Elsevier

Issue Date 

2010

Citation 

Bioresource Technology, vol. 101, no. 22, pp. 8814-8821

Keywords 

Cohnella laeviribosi HY-21Intracellular GH10 xylanaseSite-directed mutagenesisTransxylosylationXylooligosaccharides

Abstract 

The novel intracellular GH10 xylanase (iXylC) gene (1023-bp) of Cohnella laeviribosi HY-21 encoded a protein consisting of 340 amino acids with a deduced molecular mass of 39,330Da and a calculated pI of 5.81. The primary structure of iXylC was 70% identical to that of Geobacillus sp. GH10 enzyme (GenBank accession number: EDV78425). Xylanolytic activity of the His-tagged iXylC overproduced in Escherichia coli BL21 was stimulated by 2.2-fold in the presence of 0.5% non-ionic detergents. iXylC produced a mixture of xylooligosaccharides (xylobiose to xylooctaose) from xylotriose and xylotetraose used as the hydrolytic substrate. In addition, it exhibited considerable cleavage activities for p-nitrophenylxylopyranoside (PNP-xylopyranoside) and PNP-cellobioside, indicating that iXylC is a unique GH10 enzyme. The hydrolytic activity (57.8IUmL-1) of iXylC toward PNP-xylopyranoside increased to 8.3-fold by W217A and W315A mutations, while mutations of W133A, W295A, and W303A abolished the hydrolytic activity of the enzyme.

ISSN 

0960-8524

Link 

http://dx.doi.org/10.1016/j.biortech.2010.06.023

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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