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KMID : 0903519690120010033
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1969 Volume.12 No. 1 p.33 ~ p.41
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Studies on Cellulolytic Enzyme Producing by Chaetomium globosum
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Abstract
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1. Crude cellulase extracted from wheat bran media of Chaetomium globosum with pH 7.0 Mcllvaine buffer was fractionated by precipitation with ammonium sulfate and by treatment with the cellulose powder, DEAE-Sephadex A-25 and Amberite XE-65 (IRC-50) column chromatography.
2. Consquently two cellulases C-1 and C-2 were obtained by cellulose column chromatography. Cellulose C-1 was a powerful CMC-saccharifying and CMC-liquefying activity but cellulose C-2 was stronger CMC-liquefying activity compared to CMC-saccharifying activity and cellulase C-2 had smaller protein than that of cellulose C-1. And cellulose C-2 was fractionated by DEAE-Sephadex A-25 column chromatography into cellulase C-1-1 and cellulose C-1-2.
3. It can be obtained, therefore, that cellulose produced Chaelomium globosum consisted, at least, of three cellulases C-2, C-1-1 and C-1-2.
4. Cellulose C-1-1 was homogenous in the ultraviolet and the ultracentrifuge pattern. And cellulose C-1-1 had enzyme for CMC-saccharifying activity.
5. The optimum pH for the enzyme activity of cellulose C-1-1 was 4.0 in any methods of meas urement reducing sugar and viscosity. The optimum temperature was 40℃ in any methods.
6. The pH stability of cellulase C-1-1 was within pH 5.0 to pH 6.0 at 40℃ and fairly stable in acidic solution.
7. The heat stability was below 50℃ at pH 4.0 and complete heat inactivation of this cellulase occurred at 70℃.
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