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EN
Bowman-Birk inhibitors (BBI) are small serine proteinase inhibitors found in the leguminous and gramineous plants. Characteristically, their molecular masses are in the range of 6-9 kDa and are rich in disulfide bonds. The name of this family comes from the names of workers who first isolated (Bowman, 1940) and characterized (Birk, 1961) this inhibitor from soybean. Soybean BBI is the best known inhibitor of this family and it is often called ‘classical BBI’. The Bowman-Birk inhibitor is recognized as a potential cancer chemopreventive agent for humans. Human populations consuming large amounts of BBI in their diet have been demonstrated to exhibit lower rates of colon, breast, prostate and skin cancers.
PL
Badania prezentowane w niniejszej pracy miały na celu charakterystykę biochemiczną zewnątrzkomórkowej proteazy syntetyzowanej przez wyizolowany z gleby szczep Streptomyces rimosus i ocenę możliwości praktycznego wykorzystania tego enzymu w przemyśle. Badany enzym wyizolowano z 7-dniowych hodowli bakterii Streptomyces rimosus. Oczyszczony dwukrotnie enzym wykorzystano do charakterystyki biochemicznej w zakresie optymalnych warunków jego działania oraz wpływu aktywatorów i inhibitorów. Proteaza syntetyzowana przez S. rimosus wykazywała najwyższą aktywność w temperaturze 50°C i pH 7,5 oraz wysoką termostabilność w temperaturze 50°C. Dwuwartościowe jony Zn, Mo, Ni, Cd, Co hamowały aktywność enzymu, natomiast Ca i Mg – aktywowały. Silna inhibicja aktywności enzymu w obecności diizopropylofluorofosforanu (DFP) świadczy o tym, że jest to proteaza serynowa. Aktywność badanego enzymu była stabilna w obecności takich detergentów, jak Triton X-100, Tween 20, Tween 80, bromek heksadecylotrimetyloamoniowy (CTAB) oraz dodecylosiarczanu sodu (SDS).
EN
The research was aimed at isolation and biochemical characterization of the extracellular protease synthesized by the soil Streptomyces rimosus and assessment of the possibilities of practical use of this enzyme in the industry. For this purpose, the test enzyme was isolated from 7 day old culture of S. rimosus. The enzyme two-fold purified was used for biochemical characterization for optimal temperature and pH of activity and activators and inhibitors of activity. The S. rimosus protease showed the highest activity at 50°C and at pH 7.5 and high thermostability at 50°C. Divalent ions such as Zn, Mo, Ni, Cd, Co caused inhibition while Ca and Mg stimulated activity. Strong inhibition of activity in the presence of diisopropylfluorophosphate (DFP) indicates that it is a serine protease. The activity of the test enzyme was stable in the presence of such detergents as Triton X-100, Tween 20, Tween 80, hexadecyl trimethyl ammonium bromide (CTAB) and sodium dodecyl sulfate (SDS).
PL
Nakreślono rolę endogennych enzymów proteolitycznych w dojrzewaniu mięsa ryb, w procesie marynowania. Wykazano możliwość zmniejszenia strat związków azotowych uwalnianych z filetów do zalewy, przez dodatek do zalewy wielofunkcyjnych, białkowych inhibitorów proteaz, tłumiących nadmierną aktywność proteaz cyste­rnowych, aspartylowych, serynowych, w dojrzałym już mięsie. Przedstawiono dodatkowe, potencjalne funkcje tych białek, jako substancji anty-drobnoustrojowych i antyoksydacyjnych
EN
The significance of endogenous proteolytic enzymes in ageing for herrings fillets marinating process has been overviewed. The possibility of losses reduction of nitrogen components from fillets to brine by addition to brine multifunctional protein aceouspeptidase inhibitors able to diminish undesired cysteine, aspartyl, serine proteoly­sis activity in already aged meat. An antimicrobial and antioxidant factors of these proteins were also presented.
EN
Aeromonas organisms are widely distributed in aquatic environments and are also recognized as being pathogens in a variety of animals and humans. The aim of the study was to determine the effect of metal ions (Ca⁺², Cu⁺², Fe⁺², Mg⁺², Zn⁺²) and protease inhibitors (PMSF, EDTA, E-64) on the activity of Aeromonas supernatant caseinase and elastase activity. Sixteen strains of bacteria isolated from MAI/MAS diseased carp, identified as A. hydrophila (n=13) and A. sobria (n=3) were used in the study. Zinc and copper inhibited Aeromonas supernatant caseinase activity, where zinc, copper and iron inhibited elastase activity.
PL
Nasiona niektórych roślin spożywanych przez człowieka zawierają inhibitory pepsyny, a wszystkie gatunki roślin zawierają inhibitory trypsyny i chymotrypsyny. Ogrzewanie obniża aktywność tych inhibitorów.
EN
Pepsin inhibitors occur in extracts of the seeds of pumpkin, peanut, common walnut, oat, wheat, sunflower, lentil, soya and rye. Trypsin and chymotrypsin inhibitors arc contained in the extracts of the seeds of broad bean, pumpkin, bean, pea, buckwheat, barley, corn, poppy, almond, peanut, hazel nut, common walnut, oat, millet, wheat, rice, sunflower, lentil, soya, and rye. Heating the examined extracts at 100°C for 1 hour decreases the activity of these inhibitors in the degree dependent on the species and a given inhibitor specificity.
EN
The proteolytic system of insects, both its protease activities, and protease inhibitors activities, in the hemolymph and digestive tract are poorly described. The authors present protease inhibitors activities in connection with the level of antifungal activities as a part of the honeybee body surface proteolytic system. The object of the study was to compare this in castes (the queen, workers and drones), in developmental stages (eggs, larvae, pupae and imagoes) and in seasons (spring, summer and autumn). The following methods were used: protease inhibitors activity testing by the Lee and Lin method and antifungal activity testing in the presence of marker fungi on the SABG substratum. The highest protease inhibitors activities were present on the workers and the lowest ones on the queen, according to exposure to pathogens. The highest protease inhibitors activities were present during the autumn and spring. The highest protease inhibitors activities were observed in the spring in the worker larvae (16.697 U/mg) and in the mature workers (17.605 U/mg). Surface protease inhibitors activity was not observed in the drone eggs and larvae for neutral pH and in the queen larvae and pupae for neutral and alkaline pH in the summer. The larvae and pupae were found to have higher acidic protease inhibitors activity than the imagoes. The obtained results of antifungal activity presented better enthomopathogen protection in the workers and queens than in the drones. The authors have provided data connecting body surface inhibitors with antifungal cuticle protection. Our data present an initial pattern of the honeybee body surface proteolysis, and will pave the way for future biochemical studies of immunity in this insect.
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