2016
DOI: 10.15407/microbiolj78.01.013
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Purification and physico-chemical properties of Penicillium tardum α-L-rhamnosidase

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Cited by 5 publications
(8 citation statements)
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“…Whereas, in the experiment with e. erubescens, the picture changed: the same compound was shown to act as activator and its effect did not depend on the concentration and increased with time. Something similar was observed for compounds (1) and (4). They inhibited the enzyme activity from P. tardum, did not 4is an inhibitor.…”
Section: Resultssupporting
confidence: 75%
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“…Whereas, in the experiment with e. erubescens, the picture changed: the same compound was shown to act as activator and its effect did not depend on the concentration and increased with time. Something similar was observed for compounds (1) and (4). They inhibited the enzyme activity from P. tardum, did not 4is an inhibitor.…”
Section: Resultssupporting
confidence: 75%
“…In the experiments with the enzyme from e. erubescens, along with compound (3), significant activity was also observed for compounds (6) and (8), which do not contain d-metal cations, but are able to bind to the active site of a metal-containing α-L-rhamnosidase. Differences in the influence of (1)-(11) on the activity of the enzymes from P. tardum, e. erubescens and C. albidus indicate that activation and inhibition occur with the involvement of different functional groups of these enzymes.…”
Section: Resultsmentioning
confidence: 91%
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“…Раніше [1] в результаті скринінгу із колекції живих культур відділу фізіології та систематики мікроміцетів ІМВ НАН України нами був відібраний активний штам Penicillium tardum, вивчені його трофічні особливості та підібрані оптимальні умови культивування [2]. З супернатанту культуральної рідини P. tardum виділено і очищено препарат α-L-рамнозидази, вивчено його фізико-хімічні властивості [3]. Разом з тим для створення високоефективної технології отримання ензимних препаратів необхідне дослідження оптимальних параметрів α-L-рамнозидазної реакції, а також механізму дії ензиму.…”
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