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Title 

Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12

Authors 

Hyun Woo OhSun Yeon HeoDo Young KimDoo Sang ParkKyung Sook BaeHo Yong Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2008

Citation 

Antonie Van Leeuwenhoek, vol. 93, no. 4, pp. 437-442

Keywords 

cellulosimicrobium sp. HY-12exo-symbiotic bacteriumglycoside hydrolase family 10xylanase2 diethylaminoethanolamino acidbacterial enzymecalcium ioncarboxymethylcellulosecobalt

Abstract 

An exo-symbiotic bacterium capable of hydrolyzing xylan was isolated from the gut of the mole cricket, Gryllotalpa orientalis, and identified as Cellulosimicrobium sp. HY-12. The xylanase (XylACspHY-12) of this organism bound tightly to both DEAE and mono Q resins, and its molecular mass (Mr) was about 39.0 kDa. The highest xylanase activity was observed at pH 6.0 and 60°C. The enzyme was greatly suppressed by Ca2+, Cu2+, Co2+, and Fe2+ ions but not by Mg2+ and Mn2+. Although XylACspHY-12 was capable of hydrolyzing various types of xylosic compounds, it could not decompose carboxymethyl cellulose or xylobiose. The xylACspHY-12 gene consisted of an 1,188 bp open reading frame that encoded a polypeptide of 395 amino acids with a deduced molecular mass of 42,925 Da. The domain structure of XylACspHY-12 was most similar to those of the glycoside hydrolase (GH) family 10 endoxylanases. However its sequence identity with any of the enzymes in this family was below 52%. The results of this study suggest that the XylACspHY-12 is a new cellulase-free endo-β-1,4-xylanase with some properties that are distinct from those of GH family 10.

ISSN 

0003-6072

Link 

http://dx.doi.org/10.1007/s10482-007-9210-2

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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