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KMID : 0380619800120030176
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Korean Journal of Food Science and Technology
1980 Volume.12 No. 3 p.176 ~ p.181
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Comparative Studies on Immobilized Invertase on Sepharose and Phenoxyacetyl Cellulose
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최춘순/Choi, Choon Soon
변시명/전문진/Byun, Si Myung/Jeon, Moon Jin
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Abstract
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Yeast invertase was immobilized on the 2 kinds of matrices : one is an indirectly coupled enzyme to the cyanogen bromide activated Sepharose by using w-aminohexyl group as an extension arm, and the other is a tightly adsorbed enzyme on the modified hydrophobic cellulose derivative which has a phenoxyacetyl group as a linkage. The enzyme preparation coupled on Sepharose retained 26.0% of the original activity against sucrose as a substrate, while the preparation immobilized on phenoxyacetyl cellulose retained 72.9%. The immobilized invertase preparation on w-aminohexyl Sepharose showed the optimal pH 4.5, optimal temperature 60℃, activation energy 5,941 ㎈/mole ·deg and Km´ 22.2 mM against sucrose, while the preparation adsorbed on phanoxyacetyl cellulose showed the optimal pH 4.0, optimal temperature 60℃, activation energy 7,769 ㎈/mole·deg and K´ 69.9 mM.
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