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J Agric Food Chem. 2010 Jan 13;58(1):557-62. doi: 10.1021/jf902777r.

Bioproperties and purification of xylanase from Bacillus sp. YJ6.

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  • 1Department of Sea Food Science, National Kaohsiung Marine University, No. 142 Hai-Chuan Rd. Nan-Tzu, Kaohsiung 81143, Taiwan.


To characterize the xylanase from Bacillus sp. YJ6, broth after 4 days incubation at 25 degrees C was collected and purified to electrophoretical homogeneity after Sephacryl S-100 HR chromatograph. About 3.5% recovery and 678.1 purification fold were achieved. The purified xylanase, with a Mw of 19 kDa, had an optimal pH and temperature at 5.0 and 50 degrees C, respectively, and was stable at pH 5.0-9.0 or <50 degrees C. It was inhibited by Cu2+, Fe3+, Hg2+, phenylmethyl sulfonyl fluoride (PMSF), N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), N-ethylmaleimide (NEM), and leupeptin but activated by K+, Na+, Co2+, Mg2+, beta-mercaptoethanol (beta-ME), and glutathione (GSH). The purified xylanase had high specificity to beechwood, birchwood, and oat spelt xylans. The DNA fragment encoding this xylanase, corresponding to 213 amino acids, exhibited about 95% homology with seven strains of Bacillus in the NCBI database.

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