Isolation, purification and characterization of carboxymethyl cellulase (CMCase) from endophytic Fusarium oxysporum producing podophyllotoxin  

作　　者：Refaz Ahmad Dar Iram Saba Mohd Shahnawaz Manisha Kashinath Sangale Avinash Bapurao Ade Shabir Ahmad Rather Parvaiz Hassan Qazi 

机构地区：[1]Department of Botany, University of Pune, Pune, Maharashtra, India [2]Microbial Biotechnology Division, Indian Institute of Integrative Medicine (CSIR), Sanatnagar, Srinagar, Jammu and Kashmir, India

出　　处：《Advances in Enzyme Research》2013年第4期91-96,共6页酶研究进展（英文）

摘　　要：Endophytic fungus Fusarium oxysporum is a rich source of cellulases. In the present study, the highest activity was reported at 28 ° C, pH 5.6 with 2% Carboxymethyl cellulose (CMC) as carbon source. CMC was purified using Sephadex G and DEAE cellulose chromatography to 15.9 folds and the molecular weight was determined to be 84 kDa by SDS-PAGE analysis and was subsequently characterized. The purified enzyme was stable over the pH range from 4.0 to 8.0 and at temperatures below 50 ° C. The enzyme was highly active on CMC and reduced or no activity on Avicel, cellobiose and it was suggested to be CMCase/endoglucanase. The activity of endoglucanase was enhanced in the presence of MgCl2, CoCl2, FeCl3, CaCl2, FeCl2 and intensive to HgCl2. The purified enzyme showed its optimum activity at pH 5.0 - 6.0 and was quite stable at 50 ° C for 30 min and retained 45% of original activity.Endophytic fungus Fusarium oxysporum is a rich source of cellulases. In the present study, the highest activity was reported at 28 ° C, pH 5.6 with 2% Carboxymethyl cellulose (CMC) as carbon source. CMC was purified using Sephadex G and DEAE cellulose chromatography to 15.9 folds and the molecular weight was determined to be 84 kDa by SDS-PAGE analysis and was subsequently characterized. The purified enzyme was stable over the pH range from 4.0 to 8.0 and at temperatures below 50 ° C. The enzyme was highly active on CMC and reduced or no activity on Avicel, cellobiose and it was suggested to be CMCase/endoglucanase. The activity of endoglucanase was enhanced in the presence of MgCl2, CoCl2, FeCl3, CaCl2, FeCl2 and intensive to HgCl2. The purified enzyme showed its optimum activity at pH 5.0 - 6.0 and was quite stable at 50 ° C for 30 min and retained 45% of original activity.

关 键 词：ENDOPHYTE Fusarium OXYSPORUM JUNIPERUS recurva Podophyllotoxin CMCASE 

分 类 号：R73[医药卫生—肿瘤]