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Title 

Characterization of an extracellular xylanase in Panibacillus sp. HY-8 isolated from an herbivorous longicorn beetle

 

털두꺼비하늘소로부터 분리한 Panibacillus sp. HY-8이 생산하는 자일라나제의 특성

Authors 

Sunyeon heoJangryul KwakHyun Woo OhDoo Sang ParkKyung Sook BaeD H ShinHo Yong Park

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2006

Citation 

Journal of Microbiology and Biotechnology, vol. 16, no. 11, pp. 1753-1759

Keywords 

paenibacilluspurificationxylanxylanasebeetle

Abstract 

Paenibacillus sp. HY-8 isolated from the digestive tracts of the longicorn beetle, Moechotypa diphysis, produced an extracellular endoxylanase with a molecular weight of 20 kDa estimated by SDS-PAGE. The xylanase was purified to near electrophoretic homogeneity from the culture supernatant after ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The purified xylanase exhibited the highest activities at pH 6.0 and 50°C. The Km and Vmax values were 7.2 mg/ml and 16.3 U/mg, respectively, for birchwood xylan as the substrate. Nucleotide sequence of the PCR-cloned gene was determined to have the open reading frame encoding a polypeptide of 212 amino acids. The N-terminal amino acid sequence and the nucleotide sequence analyses predicted that the precursor xylanase contained a signal peptide composed of 28 amino acids and a catalytically active 19.9-kDa peptide fragment. The deduced amino acid sequence shared extensive similarity with those of the glycoside hydrolase family 11 of xylanases from other bacteria. The predicted amino acid sequence contained two glutamate residues, previously identified as essential and conserved for active sites in other xylanases of the glycoside hydrolase family 11.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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