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Immobilization of Penicillium vitale glucose-oxidase on aminosilochrome and properties of immobilized enzyme

Degtiar', R.G.; Gulyĭ, M.F.

Ukrainskii Biokhimicheskii Zhurnal 51(4): 363-368

1979

ISSN/ISBN: 0201-8470
PMID: 38549
Document Number: 143813
Penicillium vitale glucose-oxidase modified by means of the carbohydrate component oxidation is added covalently to aminoorganosylochrome. The activity of the immobilized preparations is 20-38% depending on the protein-carrier ration in immobilization. Comparison of some properties of native and immobilized glucose-oxidase showed that the rH optimum of the immobilized glucose-oxidase is slightly widened towards the alkaline regions; the immobilized glucose-oxidase possesses a considerably higher pH-stability at pH alkaline values; the immobilized glucose-oxidase preparations are characterized by a significantly greater thermostability: their thermoinactivation constant at 65 degrees C is 8-10 times lower than that of the native enzyme.

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