Full-Text Search:
Home|Journal Papers|About CNKI|User Service|FAQ|Contact Us|中文
《Food Science》 2003-05
Add to Favorite Get Latest Update

Study on Purification and Characteristics of Trichoderma reesei Cellulase

Cao Jian  
The crude cellulase of Trichoderma reesei was purified twice by ammonium sulfate fractionation, dialysis andSephadex G-100 gel filtration. The purified cellulase showed that the four distinct protein bands assayed by SDS-PAGE,showed molecular weights about 74,000、55,000、47,000、26,000, respectively. According to the molecular weight andconcentration, the four compositions were assayed as β-glucanase, CBHI, CBHII and EGI. The optimal degrading conditionsfor cellulase obtained were pH 5.0 and 50℃. The enzyme was stable between pH4.0 and 6.0, and at a temperature below 50℃.When innocubated at 70℃ for 30min, 90% of enzyme activity would be lost. When pH was beyond 8.0, almost all enzymeactivity would be lost. The enzyme activity was distinctively inhibited by metal ions such as Hg2+、Ag2+、Al3+、Pb2+ andFe3+, but enhanced by Mn2+、Co2+、Fe2+、Zn2+ and Ca2+, By Na+、Mg2+、Ba2+、Cu2+ and Ni2+ it had no significanteffect.
【CateGory Index】: Q936
Download(CAJ format) Download(PDF format)
CAJViewer7.0 supports all the CNKI file formats; AdobeReader only supports the PDF format.
©2006 Tsinghua Tongfang Knowledge Network Technology Co., Ltd.(Beijing)(TTKN) All rights reserved