Th. Alrawi, A., ASW, , B.A. Alani, I. (2007). CELLULASES PRODUCTiON FROlVI LOCAL ASPERGILLUS SP. ISOLATE AND ASSESING SOME OF THEIR PROPERTIES AND APPLICATIOS 2-PURIFICATION OF CELLULASES AND CELLOBIASE FRO;VI ASPERGILLUS SP. AI8. , 38(3), 36-42.
Akrarn Th. Alrawi; ASW; Il B.A. Alani. "CELLULASES PRODUCTiON FROlVI LOCAL ASPERGILLUS SP. ISOLATE AND ASSESING SOME OF THEIR PROPERTIES AND APPLICATIOS 2-PURIFICATION OF CELLULASES AND CELLOBIASE FRO;VI ASPERGILLUS SP. AI8". , 38, 3, 2007, 36-42.
Th. Alrawi, A., ASW, , B.A. Alani, I. (2007). 'CELLULASES PRODUCTiON FROlVI LOCAL ASPERGILLUS SP. ISOLATE AND ASSESING SOME OF THEIR PROPERTIES AND APPLICATIOS 2-PURIFICATION OF CELLULASES AND CELLOBIASE FRO;VI ASPERGILLUS SP. AI8', , 38(3), pp. 36-42.
Th. Alrawi, A., ASW, , B.A. Alani, I. CELLULASES PRODUCTiON FROlVI LOCAL ASPERGILLUS SP. ISOLATE AND ASSESING SOME OF THEIR PROPERTIES AND APPLICATIOS 2-PURIFICATION OF CELLULASES AND CELLOBIASE FRO;VI ASPERGILLUS SP. AI8. , 2007; 38(3): 36-42.

CELLULASES PRODUCTiON FROlVI LOCAL ASPERGILLUS SP. ISOLATE AND ASSESING SOME OF THEIR PROPERTIES AND APPLICATIOS 2-PURIFICATION OF CELLULASES AND CELLOBIASE FRO;VI ASPERGILLUS SP. AI8

The Iraqi Journal of Agricultural Science
Article 1, Volume 38, Issue 3, 2007, Pages 36-42
Authors
Akrarn Th. Alrawi; ; Il B.A. Alani
Abstract
The cellulytic enzymes produced by Aspergillus .ljJ.A,s by solid state fermentation were purified by four steps iuclllding precipitation with 40% ammonium sulphate followed by gel filtration cnromatogrnphy (Sephade x G-200) (6o.d.5 ern), it was eluted by phcsphate buffer (0.2 ~I) pH=8.0 with NaCI (0.05 ~I). Two proteins were found .- and B each one had two enzymes (cellulase and cellubiasej.Thc protein 13 (which contained cellulase Bel and cellubiase Bcb) was choused for further purification to homogeneity by dialysis against phosphate buffer (0.0 I M) and ion exchanger chromatogr-aphy (DEAE - Scphad ex .-50) (8x2.2 ern), the enzymes obtained were unconjugarcd ccllubiase BCb I and conjugated cellubinsc BCb2 and just one conjugated cellulase BCI. BCI and BCb2 had been choosed for further studying. their purification fold were 41.2-1 for BCI and 32.83 for BCb2, their yield were 65.25% and 35.09°;', respectively, the specific activity for them were 129.5 lJ/rng and 157.54 U/rng, respectively. In conclusion, we can say that cellulases arc enzymatic system eontaining many enzymes that may had the same molecular weight with diff'ercnt net charge, we can separate them by using above techniques in order to distinguish between them if it is exoglucanase or enrloglucnnasc.
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