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Wyszukujesz frazę "β-galactosidase" wg kryterium: Temat


Wyświetlanie 1-9 z 9
Tytuł:
Influence of Ionic Liquids on growth of Escherichia coli strain possessing β-galactosidase activity
Autorzy:
Stobińska, M.
Urbański, D.
Bartkowiak, A.
Powiązania:
https://bibliotekanauki.pl/articles/115739.pdf
Data publikacji:
2013
Wydawca:
Fundacja na Rzecz Młodych Naukowców
Tematy:
ionic liquids
β-galactosidase
toxicity
Opis:
Ionic liquids (ILs) have gained a significant attention as alternative solvents in many chemical and biological reactions. ILs have evolved as a new type of non-aqueous solvents for biocatalysis, because they can stabilize and activate enzymes. Ionic liquids to be considered as so called “green solvents” should possess only very low or no toxicity to living organism and the environment. Currently, very little is known about the biotoxicity of ionic liquids. Within this paper a relative toxicity of two ionic liquids 1,3 dimethylimidazolium methyl sulfate [MMIM][MeSO4] and 1-hexyl-3-methylimidazolium chloride [HMIM][Cl]) on the growth of Escherichia coli (E.coli) was evaluated. In this study we focused on ionic liquids, which potentially could increase activity of β-galactosidase produced by selected strain of E. coli. The inhibition of cell growth in the presence of various ionic liquids was determined using both, solid and liquid cultures. Liquid culture was incubated in culture medium with different concentrations of ionic liquids (0.1, 1, 5, 10% (v/v)). Determination of the minimal inhibitory concentration (MIC50) of ionic liquids was based on monitoring of E. coli growth by optical density measured at 600 nm using densitometer. In the second method the solid culture plate with addition of various amount of ILs has been used. The number of colonies formed on the solid culture plate was converted to colony forming units (CFUs). The obtained results have confirmed, that prescreening based on cytotoxicity tests is a key element in selection procedure of ILs for any biotechnological processes based on application of microorganisms.
Źródło:
Challenges of Modern Technology; 2013, 4, 1; 38-40
2082-2863
2353-4419
Pojawia się w:
Challenges of Modern Technology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Low-glucose medium induces ORP150 expression and exerts inhibitory effect on apoptosis and senescence of human breast MCF7 cells
Autorzy:
Krętowski, Rafał
Stypułkowska, Anna
Cechowska-Pasko, Marzanna
Powiązania:
https://bibliotekanauki.pl/articles/1039569.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
β-galactosidase
senescence
ORP150
apoptosis
Opis:
Glucose deprivation is a factor evoking endoplasmic reticulum (ER) stress and induction of expression of an oxygen-regulated protein of 150 kDa (ORP150). We studied the effect of inducible overexpression of ORP150 on senescence and apoptosis of human breast carcinoma cells (MCF7) and human skin fibroblasts. We found an inhibitory effect of ORP150 on apoptosis and senescence of MCF7 cells, but not fibroblasts in ER stress conditions. An increased expression of senescence-associated β-galactosidase and acid β-galactosidase activity (biomarkers of cellular senescence) was observed. We suggest that ORP150 induction in cancer cells can promote tumour progression and may be a major cause of their resistance to chemotherapeutics.
Źródło:
Acta Biochimica Polonica; 2013, 60, 2; 167-173
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Future applications of apricot (Prunus armeniaca kaisa) ß galactosidase in dairy industry
Autorzy:
Ansarin, S. A
Satar, R.
Zaidi, S. K.
Khan, M. J.
Naseer, M. I.
Al-Qahtani, M. H.
Maskat, M. Y.
Powiązania:
https://bibliotekanauki.pl/articles/779412.pdf
Data publikacji:
2014
Wydawca:
Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
Tematy:
apricot
β galactosidase
lactose hydrolysis
dairy industries
Opis:
The present study demonstrates the immobilization of β galactosidase from apricots (Prunus armeniaca kaisa) on an inexpensive concanavalin A layered cellulose-alginate hybrid gel. Immobilized β galactosidase retained 78% of the initial activity after crosslinking by glutaraldehyde. It exhibited greater fraction of activity at both acidic and basic pH, and showed broad spectrum temperature optimum as compared to free enzyme. Moreover, immobilized enzyme exhibited higher thermal stability at 60oC and retained 80% of the original enzyme activity in presence of 3% galactose. The crosslinked immobilized enzyme showed improved hydrolysis of lactose from milk and whey in batch processes at 50oC as well as in continuous reactors operated at flow rate of 20 mL/h and 30 mL/h even after one month. Moreover, crosslinked adsorbed β galactosidase retained 76% activity even after its sixth repeated use, thereby promoting its use for lactose hydrolysis in various dairy products even for longer durations.
Źródło:
Polish Journal of Chemical Technology; 2014, 16, 3; 74-79
1509-8117
1899-4741
Pojawia się w:
Polish Journal of Chemical Technology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Determination of lysosomal exoglycosidases in human saliva
Autorzy:
Chojnowska, Sylwia
Zalewska, Anna
Knaś, Małgorzata
Waszkiewicz, Napoleon
Waszkiel, Danuta
Kossakowska, Agnieszka
Zwierz, Krzysztof
Powiązania:
https://bibliotekanauki.pl/articles/1039339.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
β-galactosidase
β-glucuronidase
α-fucosidase
α-mannosidase
N-acetyl-β-D-hexosaminidase
saliva
Opis:
Background: Currently we observe a growing interest in human saliva as a non-invasive material for diagnosis and monitoring of general and oral diseases. Methods: The aim of our study was adaptation of the Marciniak et al. (Marciniak J, Zalewska A, Popko J, Zwierz K, 2006, Clin Chem Lab Med 44: 933-937) method for determination of HEX and GLU activity in synovial fluid, and for determination of: HEX and GLU, as well as MAN, GAL, and FUC activity in human saliva. Results: Under optimal conditions, 10 μl of saliva for HEX, and 30 μl for GLU, MAN, GAL and FUC, were sufficient for determination of human salivary exoglycosidases activity with variation coefficient ranging from 0.89 for GLU to 0.99 for GAL. Conclusion: The adapted method for exoglycosidases activity determination in human saliva is sufficiently sensitive and precise to use in clinical diagnosis.
Źródło:
Acta Biochimica Polonica; 2014, 61, 1; 85-90
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Activity of lysosomal exoglycosidases in submandibular glands of rats intoxicated by cadmium at doses related to human chronic environmental and occupational exposures.
Autorzy:
Zalewska, Anna
Brzó;ska, Małgorzata
Marciniak, Justyna
Karaszewska, Katarzyna
Zwierz, Krzysztof
Moniuszko-Jakoniuk, Janina
Powiązania:
https://bibliotekanauki.pl/articles/1041566.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
exoglycosidases
β-galactosidase
α-mannosidase
cadmium
salivary glands of rats
β-N-acetylhexosaminidase
Opis:
Work in cadmium (Cd) smelter and smoking cigarettes damages teeth and oral mucosa which are protected by tissue and salivary glycoconjugates: glycoproteins, glycolipids, and proteoglycans. We worked out a rat model imitating human "environmental" and "occupational" exposure to cadmium using 5 mg Cd and 50 mg Cd/l in drinking water, respectively. In submandibulary glands of exposed to Cd rats, we found the time and dose dependent accumulation of Cd and simultanous decrease in activity of β-N-acetylhexosaminidase (HEX). In homogenates of submandibulary glands of control rats, β-N-acetylhexosaminidase showed the highest activity. The activities of α;-mannosidase and β-galactosidase were very low. None of these exoglycosidases were inhibited by Cd even at 44 mM concentration.
Źródło:
Acta Biochimica Polonica; 2004, 51, 3; 831-837
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Graphene oxide flake activation via divinylsulfone – a procedure for efficient β-galactosidase immobilization
Autorzy:
Trusek, Anna
Powiązania:
https://bibliotekanauki.pl/articles/779087.pdf
Data publikacji:
2019
Wydawca:
Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
Tematy:
graphene oxide
enzyme chemical immobilization
divinylsulfone
β-galactosidase
lactose-free product
Opis:
Flaky graphene oxide was activated with divinylsulfone followed by immobilization of the β-galactosidase enzyme. An active and stable preparation was obtained. β-galactosidase stability after immobilization was much higher than with the native enzyme. The half-life time of the immobilized enzyme was estimated as 165 hours, while for the native form, the estimate was only 5 hours. The developed procedure for the preparation of flaked graphene and its use in the chemical immobilization of enzymes can be used for any enzyme. A processing solution for continuous operation was proposed and verified using cow’s milk, with lactose as the hydrolysed substrate, as a dosing stream. Lactose, a milk sugar, was effectively hydrolysed. Product for allergy sufferers who cannot digest lactose has been obtained in this way.
Źródło:
Polish Journal of Chemical Technology; 2019, 21, 1; 27-32
1509-8117
1899-4741
Pojawia się w:
Polish Journal of Chemical Technology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Temperature effect on properties of β-galactosidase entrapped in alginate matrix: an experimental research supported by molecular modeling
Wpływ temperatury na właściwości β-galaktozyadazy inkludowanej w matrycy alginianowej: badania eksperymentalne wspomagane molekularnym modelowaniem
Autorzy:
Labus, K.
Radosiński, Ł.
Kuchta, B.
Trusek-Hołownia, A.
Powiązania:
https://bibliotekanauki.pl/articles/2073108.pdf
Data publikacji:
2015
Wydawca:
Stowarzyszenie Inżynierów i Techników Mechaników Polskich
Tematy:
β-galactosidase
alginate
immobilization
temperature
molecular dynamics
β-galaktozydaza
alginian
immobilizacja
temperatura
dynamika molekularna
Opis:
The current study was separated into two parts: experimental study of temperature impact on activity and stability of immobilized β-galactosidase and preliminary modeling of changes generated in alginate-Ca2+ matrix with respect to temperature using molecular dynamics approach. On the basis of obtained results it can be stated that combination of experimental research and computer simulations on molecular level provides an additional insight greatly enhancing capabilities to control and optimize the process using immobilized biocatalyst.
Badania składały się z dwu części: eksperymentalnego wyznaczenia wpływu temperatury na właściwości immobilizowanej β-galaktozydazy oraz wstępnego modelowania dynamiki zmian w strukturze matrycy alginian-Ca2+ w zależności od temperatury na poziomie molekularnym. Na podstawie uzyskanych wyników można stwierdzić, że takie połączenie badań eksperymentalnych z symulacjami komputerowymi na poziomie cząsteczkowym pozwala na uzyskanie bardziej szczegółowej wiedzy na temat dynamiki układu, co w konsekwencji stwarza możliwość lepszej kontroli i optymalizacji procesu prowadzonego z wykorzystaniem immobilizowanego enzymu.
Źródło:
Inżynieria i Aparatura Chemiczna; 2015, 3; 98--100
0368-0827
Pojawia się w:
Inżynieria i Aparatura Chemiczna
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Thermostable Pyrococcus woesei β-D-galactosidase - high level expression, purification and biochemical properties
Autorzy:
Wanarska, Marta
Kur, Józef
Pladzyk, Radosław
Turkiewicz, Marianna
Powiązania:
https://bibliotekanauki.pl/articles/1041317.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Pyrococcus woesei
β-d-galactosidase
Escherichia coli
purification
expression system
Opis:
The gene encoding β-D-galactosidase from Pyrococcus woesei was PCR amplified, cloned, expressed in Escherichia coli under the control of an inducible T7 promoter, purified and characterized. The expression system was developed by the construction of recombinant plasmid, based on the high copy number pUET1 vector, giving four times more efficient expression of P. woesei β-D-galactosidase (20 mg of enzyme from 1 liter of culture) than that obtained from a previously constructed one. The recombinant enzymes were purified in a two-step procedure: double heat-denaturation of E. coli cell proteins and affinity chromatography on p-aminobenzyl 1-thio-β-D-galactopyranoside-agarose. To achieve efficient purification of P. woesei β-D-galactosidase by immobilized metal-ion affinity chromatography (IMAC), a His-tag was placed either at the N- or the C-terminal of the coding sequence. The obtained fusion proteins revealed the same specific activity of approximately 5400 U/mg, which was 10 times lower than the wild-type β-D-galactosidase (51100 U/mg). The activity of P. woesei β-D-galactosidase was enhanced by thiol compounds, Mg2+ ions and D-galactose, and was inhibited by heavy metal ions and D-glucose, while Ca2+ ions had no effect.
Źródło:
Acta Biochimica Polonica; 2005, 52, 4; 781-787
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Immobilization of Aspergillus oryzae Β galactosidase on concanavalin A-layered calcium alginate-cellulose beads and its application in lactose hydrolysis in continuous spiral bed reactors
Autorzy:
Ansari, S. A
Husain, Q.
Powiązania:
https://bibliotekanauki.pl/articles/779751.pdf
Data publikacji:
2011
Wydawca:
Zachodniopomorski Uniwersytet Technologiczny w Szczecinie. Wydawnictwo Uczelniane ZUT w Szczecinie
Tematy:
Β galaktozydazy
unieruchomienie
celulozowy alginian
konkanawalina A
reaktor spiralny
hydroliza laktozy
β-galactosidase
immobilization
cellulose-alginate
concanavalin A
spiral bed reactor
lactose hydrolysis
Opis:
In this study, Aspergillus oryzae Β galactosidase was immobilized on concanavalin A layered calcium alginate-cellulose beads as a bioaffi nity support. Immobilized enzyme showed a remarkable broadening in temperature-activity profi les as compared to the native enzyme and exhibited 65% activity in the presence of 5% galactose. Michaelis constant (Km) was 2.57 mM and 5.38 mM for the free and the immobilized Β galactosidase, respectively. Crosslinked Β galactosidase showed greater catalytic activity in the presence of Mg2+ and was more stable during storage at 4°C for 6 weeks. Immobilized enzyme hydrolyzed 67% lactose in milk in 8 h and 85% lactose in whey in 9 h in the stirred batch process at 50oC. The continuous hydrolysis of lactose by crosslinked Β galactosidase in spiral bed reactor exhibited 93% and 88% hydrolysis of lactose at flow rate of 20 ml/h and 30 ml/h, after 1 month operation, respectively.
Źródło:
Polish Journal of Chemical Technology; 2011, 13, 4; 15-20
1509-8117
1899-4741
Pojawia się w:
Polish Journal of Chemical Technology
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-9 z 9

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