Abstract
Исследован механизм воздействия УФ-излучения на трипсин, иммобилизованный на матрице среднемолекулярного (200 кДа) и высокомолекулярного (350 кДа) хитозанов. Установлено, что ферментативная активность молекул иммобилизованного трипсина под воздействием УФ-излучения практически не подвержена изменению. Выдвинуто предположение о фотопротекторном эффекте матрицы хитозана. Выявлено, что при дозе 6040 Дж/м2 происходят изменения в структуре белкового комплекса, связаные с варьированием количества неупорядоченных структур и β-слоев в молекуле фермента, –СОО– колебаниями аминокислот, проявляющиеся в снижении активности препарата.
Highlights
Today the solution of theoretical and practical issues related to understanding the mechanism of UV light action on biosystems of various organization levels, patterns of UV induced changes in the structural and functional characteristics of immobilized enzymes remains relevant
We have investigated the mechanism of the UV light action on trypsin immobilized on the chitosan matrix, since for immobilized enzymes, the number of possible inactivating pathways is substantially less than in the case of soluble proteins
Two types of chitosan served as carriers for immobilization: medium molecular weight (200 kDa) and high molecular weight (350 kDa)
Summary
Today the solution of theoretical and practical issues related to understanding the mechanism of UV light action on biosystems of various organization levels, patterns of UV induced changes in the structural and functional characteristics of immobilized enzymes remains relevant. For a more detailed study of photoprocesses originating from the adsorbed chitosan matrix with trypsin under the action of UV light were investigated IR-spectra of the immobilized enzyme after exposure to UV-irradiation at doses
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