Partial Purification and Characterization of Cellulase (Ec.3.2.1.4) from Aspergillus niger Using Saw Dust as Carbon Source

2017 ◽  
Vol 06 (01) ◽  
Author(s):  
Ekpa Emmanuel ◽  
Adebisi Queen
2010 ◽  
Vol 4 (2) ◽  
pp. 78-85
Author(s):  
Jasim M. Awdaa

Inulinase was produced from local isolate of Aspergillus niger J3. The inulinase was purified by two steps included precipitation by amonium sulphate at (30-80) % sa-turation and gel filtration on sephadex G100. The final purification folds and the yield of the enzyme were 3.15 times and 28.24%, respectively. The purified enzyme has the following characteristics: The optimum pH of the enzyme activity was 5.5. The enzyme was most stable at pH (4.5 - 6). The optimum temperature for its activity was 45c. The enzyme retained its original activity when incubates at (30-55) c for 20 minutes. Mercury chloride inhibited the enzyme completely at concentration of 10mM, cupper sulphate and calisium chloride inhibited the enzyme at concentrations of 85% and 7% respectively. It was revealed that the enzyme had the efficiency to hydrolyze 87% of 5% inulin solution when treated at 45c for 120 min.


2002 ◽  
Vol 67 (6) ◽  
pp. 2016-2022 ◽  
Author(s):  
C. Vignaud ◽  
N. kaid ◽  
L. Rakotozafy ◽  
S. Davidou ◽  
J. Nicolas

2009 ◽  
Vol 25 (12) ◽  
pp. 2095-2102 ◽  
Author(s):  
Georgi Dobrev ◽  
Boriana Zhekova ◽  
Ginka Delcheva ◽  
Lidia Koleva ◽  
Nicola Tziporkov ◽  
...  

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