›› 2002, Vol. 45 ›› Issue (2): 165-169.

• RESEARCH PAPERS • Previous Articles     Next Articles

Purification and properties of xylanase from Anoplophora chinensis (Forster)

DONG Ya-Min, YIN You-Ping1*, CAO Yue-Qing, HE Zheng-Bo   

  • Online:2002-04-20 Published:2002-04-20

Abstract: A xylanase was purified from the homogenate of alimentary canal of Anoplophora chinensis (Froster) by acetone precipitation, Q-Sepharose ion-exchange chromatography and preparative PAGE. The xylanase had a molecular mass approximate 25 kD and pI 4.0. For the action of the enzyme isolated, the most optimal temperature and pH were 50℃ and 5.4 respectively. About 60% of the enzyme activity remained after incubating it at 50℃ for 2 hours. The enzyme could be inhabited by Hg2+,MnO-4,SDS, Cu2+, Mn2+, Ag+, Zn2+, Pb+ and Urea. It could hydrolyse carboxymethylcellulose (CMC). The enzyme had a Km of 2.47 mg/mL and a Vmax of 0.6 IU/mL for birchwood xylan at 50℃ and pH 4.4

Key words: Anoplophora chinensis (Forster), xylanase, purification, properties