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Purification and Partial Amino Acid Sequence of Xylanase from Aspergillus phoenicis

JIANG Jun-Ping;YAN Zi-Zheng and ZHANG Shu-Zheng(Institute of Microbiology, Academia Sinica,Beijing 100080)  
Xylanase from Aspergillus phoenicis was purified by(NH4)2SO4 fractionation,gel filtration on Sephadex G-100, ion exchange chromatography on DEAESphadex A-50 and HPLC.The enzyme was homogeneous when examined by PAGE,SDS-PAGE,HPLC as well as zymogram on RBB-xylan.No sulphydryl groups and disulphides bridge were detected with DTNB.The sequences of 14 amino acids at N-terminus and 6 amino acids at C-terminus were determined.The amino-terminal sequence showed extensive homology with the sequences of other 6 xylanases and possessed a proposed consensus structure:…Thr…Gly…Gly…Tyr….The carboxyl-terminal sequence was also related to that of other 2 xylanases.
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