Immobilization of Penicillium vitale glucose-oxidase on aminosilochrome and properties of immobilized enzyme
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 imm...
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Veröffentlicht in: | Weekly epidemiological record 1979-07, Vol.51 (4), p.363-368 |
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creator | Degtiar', R G Gulyĭ, M F |
description | 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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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.</description><identifier>ISSN: 0201-8470</identifier><language>ukr</language><ispartof>Weekly epidemiological record, 1979-07, Vol.51 (4), p.363-368</ispartof><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids></links><search><creatorcontrib>Degtiar', R G</creatorcontrib><creatorcontrib>Gulyĭ, M F</creatorcontrib><title>Immobilization of Penicillium vitale glucose-oxidase on aminosilochrome and properties of immobilized enzyme</title><title>Weekly epidemiological record</title><description>Penicillium vitale glucose-oxidase modified by means of the carbohydrate component oxidation is added covalently to aminoorganosylochrome. 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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.</abstract></addata></record> |
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ispartof | Weekly epidemiological record, 1979-07, Vol.51 (4), p.363-368 |
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language | ukr |
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source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
title | Immobilization of Penicillium vitale glucose-oxidase on aminosilochrome and properties of immobilized enzyme |
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