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KMID : 0903519810240030186
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1981 Volume.24 No. 3 p.186 ~ p.193
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Purification and Characterization of Cellulolytic Enzymes from Aspergillus niger
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Abstract
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Three fractions of carboxymethyl-cellulase (F-Ⅰ, F-Ⅱ, and F-Ⅲ) and β-glucosidase form Aspergillus uiger were partially purified by ammonium sulfare fractionation. Sephadex G-150 and DEAE Sephadex column chromatography. The optimum conditions such as pH and temperature and thermal inactivation properties of the enzymes were investigated. Arrhenius plots of F-Ⅱ and F-Ⅲ appeared as straight lines, whereas that of F-Ⅰ was biphasic. The Z-values of F-Ⅱ and F-Ⅲ were 8℃ and 10℃ respectively, while that of F-I was 4℃ over 60∼70℃ and 383℃ over 70∼98℃. Three fractions and the crude extract of carboxymethyl-cellulase exhibited a similar optimum pH 4.3 and temperature of 60℃, while Z-value of crude activity of both purified and crude extract of β-glucosidase was shown at pH 4.7 and 60℃, and z-value of the enzyme was 7℃.
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