Catalytic activity and the stability of horseradish peroxidase increase as a result of its incorporation into a polyelectrolyte complex with chitosanстатья
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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Авторы:
Veselova I.A. ,
Kireiko A.V. ,
Shekhovtsova T.N.
Журнал:
Applied Biochemistry and Microbiology
Том:
45
Номер:
2
Год издания:
2009
Издательство:
Maik Nauka/Interperiodica Publishing
Местоположение издательства:
Russian Federation
Первая страница:
125
Последняя страница:
129
DOI:
10.1134/S0003683809020021
Аннотация:
The incorporation of horseradish peroxidase into polyelectrolyte complexes with chitosans of different molecular weights (MW 5-150 kDa) yielded highly active and stable enzyme preparations. As a result of the selection of optimal conditions for the formation of peroxidase-chitosan complexes, it was found that 0.1% chitosan with a MW of 10 kDa had the strongest activatory effect on peroxidase (activation degree, >70%) in the reaction of o-dianisidine oxidation by hydrogen peroxide. The complex formed by 0.001% chitosan with a molecular weight of 150 kDa was most stable: when immobilized on foamed polyurethane, it retained at least 50% of the initial activity for 550 days. The highest catalytic activity was exhibited in a 0.05 M phthalate buffer (pH 5.9-6.2) by the complex containing 0.006-0.009% chitosan in the indicator reaction. The activatory effect of the polysaccharide on the enzyme was determined by its influence on the binding and conversion of the reducting substrate peroxidase. © 2009 Pleiades Publishing, Ltd.
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