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Title 

Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116

Authors 

Min-Soo KimMi Hee WooYoung Hyo ChangN ChungJoong Su Kim

Publisher 

Springer

Issue Date 

2016

Citation 

Applied Biological Chemistry, vol. 59, no. 2, pp. 313-320

Keywords 

Glycosyl hydrolase family 10Paenibacillus spSaccharificationXylanaseΒ-glucosidase

Abstract 

In our present study, a new Endo-1,4-β-xylanase (EC 3.2.1.8) was isolated, which belongs to glycosyl hydrolase family 10 member. The new enzyme designated as xynA was expressed for biochemical characterization. The xynA xylanase was identified in Paenibacillus sp. EC116. The novel gene had the size of 2673 base pairs, which correspond to 891 amino acid residues. The expressed enzyme has a size of ~100?kDa. The amino acid sequence was similar to that of endo-1,4-beta-xylanase from Paenibacillus sp. FSL R5-192 (ETT36211.1) (96?% identical). The xylanase has an optimal temperature of 40?°C and the pH optimum of 6.0. The specific activity of the xylanase toward birchwood xylan was about 0.69?μmol?min?1 mg?1, the Vmax value of 1.639?μmol?mg?1 min?1, and the Km value of 35.1?mg?ml?1. The EC116 xylanase was relatively stable up to 60?°C. Xylanase enzymes have numerous industrial applications, which need to meet the specific requirements for each application. We hope that our EC116 xylanase is one of the candidates for commercial applications

ISSN 

2468-0834

Link 

http://dx.doi.org/10.1007/s13765-016-0159-6

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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