상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

First thermostable endo-beta-1,4-glucanase from newly isolated Xanthomonas sp. EC102

 

Xanthomonas sp. EC102로 부터 신규 내열성 Endo-beta-1,4-glucanase 분리

Authors 

Mi-Hee WooYoung Hyo ChangH S LeeP J PakJoong Su KimN Chung

Publisher 

Springer Verlag (Germany)

Issue Date 

2014

Citation 

Protein Journal, vol. 33, no. 0, pp. 110-117

Keywords 

CharacterizationEndoglucanaseThermostabilityXanthomonas sp.

Abstract 

A novel gene encoding thermostable endoglucanase was identified in Xanthomonas sp. EC102 from soil. The gene had 1,458 base pairs of open reading frame, which encode a 52-kDa protein of 486 amino acid residues. Sequence of the amino acid residues was similar with the endoglucanase from Xanthomonas campestris pv. campestris ATCC33913 (GenBank Accession No. NP_638867.1) (94 % identity). The endoglucanase was overexpressed in Escherichia coli BL21 and purified. Temperature for the highest enzymatic activity was 70 °C and pH optima was pH 5.5. The specific activity of the endoglucanase toward carboxymethylcellulose (CMC) was approximately 2 μmol min-1 mg-1, Vmax for CMC was 1.44 μmol mg-1 min-1, and Km values was 25.6 mg mL-1. The EC102 endoglucanase was stable at temperatures up to 60 °C, and it was activated by 0.1 mM of Mn2+ and Co2+. This is the first report about thermostable endoglucanase from Xanthomonas sp.

ISSN 

1572-3887

Link 

http://dx.doi.org/10.1007/s10930-013-9535-9

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)