Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

English (EN)·Polski (PL)·Yкраїнський (UK)
Przejdź do strony domowej biblioteki Centralna Biblioteka Wojskowa Link otwiera się w nowym oknie Logo biblioteki Prolib Integro - strona głównaCentralna Biblioteka Wojskowa

Wyszukujesz frazę "3-glucanase" wg kryterium: Temat

  Lista filtrów
Wyrównaj
    Wyświetlanie 1-5 z 5
    Tytuł:
    Cell wall-degrading enzymes and aggressiveness in Stagonopspora nodorum
    Autorzy:
    Cui, K. R.
    Krupinsky, J. M.
    Dai, Q.
    Arseniuk, E.
    Ueng, P. P.
    Powiązania:
    https://bibliotekanauki.pl/articles/2198866.pdf
    Data publikacji:
    2005-06-23
    Wydawca:
    Instytut Hodowli i Aklimatyzacji Roślin
    Tematy:
    aggressiveness
    β-1,3-glucanase
    cellulase
    isozymes
    isoelectric focusing
    pectinase
    secretion
    Stagonospora nodorum
    xylanase
    Opis:
    Stagonospora nodorum produces cell wall degrading enzymes when grown in culture media containing cell wall components. The pathogen grew as well on minimal agar plates containing cellulose, xylan and pectin as glucose, except having sparser mycelia. Four cell wall-degrading enzymes, cellulase, xylanase, pectinase and b-1,3-glucanase were coordinately induced in culture filtrates growing on xyaln and cellulose as substrates. An aggressive isolate (sn26-1) secreted more cell wall-degrading enzymes than the others. Based on isoelectric focusing profiles, six to seven xylanase isozymes were induced by cellulose and xylan. No difference was found in the high (sn26-1) and low (9074) aggressive isolates. Addition of cell wall-degrading enzyme mixtures, not high xylanase alone, to a spore suspension of a low aggressive isolate (9074) caused a limited increase in tissue necrosis. We conclude that the cell wall degrading enzymes play a role in early penetration of the host by the fungus, but they are not important elicitors for disease development.
    Źródło:
    Plant Breeding and Seed Science; 2005, 51; 21-30
    1429-3862
    2083-599X
    Pojawia się w:
    Plant Breeding and Seed Science
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Conserved Cys residue influences catalytic properties of potato endo-(1→3)-β-glucanase GLUB20-2
    Autorzy:
    Witek, Agnieszka
    Witek, Kamil
    Hennig, Jacek
    Powiązania:
    https://bibliotekanauki.pl/articles/1040688.pdf
    Data publikacji:
    2008
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    GLUB20-2
    inhibition
    endo-(1→3)-β-glucanase
    Solanum tuberosum
    structure-function relationships
    substrate specificity
    Opis:
    The synthesis and degradation of (1→3)-β-glycosidic bonds between glucose moieties are essential metabolic processes in plant cell architecture and function. We have found that a unique, conserved cysteine residue, positioned outside the catalytic centre of potato endo-(1→3)-β-glucanase - product of the gluB20-2 gene, participates in determining the substrate specificity of the enzyme. The same residue is largely responsible for endo-(1→3)-β-glucanase inhibition by mercury ions. Our results confirm that the spatial adjustment between an enzyme and its substrate is one of the essential factors contributing to the specificity and accuracy of enzymatic reactions.
    Źródło:
    Acta Biochimica Polonica; 2008, 55, 4; 791-797
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Purification and properties of an α-(1 → 3)-glucanase (EC 3.2.1.84) from Trichoderma harzianum and its use for reduction of artificial dental plaque accumulation
    Autorzy:
    Wiater, Adrian
    Pleszczyńska, Małgorzata
    Rogalski, Jerzy
    Szajnecka, Lucyna
    Szczodrak, Janusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1039622.pdf
    Data publikacji:
    2013
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    streptococcal film
    Trichoderma harzianum
    mutanase
    purification
    α-(1 → 3)-glucanase
    Opis:
    Extracellular α-(1 → 3)-glucanase (mutanase, EC 3.2.1.84) produced by Trichoderma harzianum CCM F-340 was purified to homogeneity by ultrafiltration followed by ion exchange and hydrophobic interaction chromatography, and final chromatofocusing. The enzyme was recovered with an 18.4-fold increase in specific activity and a yield of 4.3%. Some properties of the α-(1 → 3)-glucanase were investigated. The molecular mass of the enzyme is 67 kDa, as estimated by SDS/PAGE, its isoelectric point 7.1, and the carbohydrate content 3%. The pH and temperature optima are 5.5 and 45°C, respectively. The enzyme is stable over a pH range of 4.5-6.0 and up to 45°C for 1 h. The Km and Vmax under standard assay conditions are 0.73 mg/ml and 11.39 x 10-2 µmol/min/mg protein, respectively. The enzyme activity is stimulated by addition of Mg2+ and Na+, and significantly inhibited by Hg2+. The α-(1 → 3)-glucanase preparation preferentially catalyzed the hydrolysis of various streptococcal mutans and fungal α-(1 → 3)-glucans. The 20-residue N-terminal sequence of the enzyme is identical with those of other α-(1 → 3)-glucanases from the genus Trichoderma, and highly similar to those from other fungi. The purified α-(1 → 3)-glucanase was effective in preventing artificial dental plaque formation. The easy purification from fermentation broth and high stability, and the effective inhibition of oral biofilm accumulation make this α-(1 → 3)-glucanase highly useful for industrial and medical application.
    Źródło:
    Acta Biochimica Polonica; 2013, 60, 1; 123-128
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Mikrobiologiczne wytwarzanie białka o aktywności β-glukanazy
    Microbiological production of protein with β-glucanase activity
    Autorzy:
    Zasłona, H.
    Trusek-Hołownia, A.
    Powiązania:
    https://bibliotekanauki.pl/articles/2073107.pdf
    Data publikacji:
    2015
    Wydawca:
    Stowarzyszenie Inżynierów i Techników Mechaników Polskich
    Tematy:
    fermentacja wgłębna
    β-1,3-glukanaza
    hydroliza CM-kurdlanu
    stabilność operacyjna
    submerged fermentation
    β-1,3-glucanase
    CM-curdlan hydrolysis
    operational stability
    Opis:
    W pracy przedstawiono produkcję enzymu degradującego niektóre rodzaje hemicelulozy. Białko zostało wyprodukowane przez zmodyfikowany genetycznie szczep E. coli w reaktorze mikrobiologicznym. Wskazano optymalne warunki prowadzenia procesu biosyntezy białka. Wyznaczono stałą szybkości reakcji preparatu oczyszczonego. Określono stabilność operacyjną enzymu będącą kluczowym parametrem dla potencjalnego zastosowania w procesie wielkotonażowym hydrolizy komponentów biomasy roślinnej.
    The paper presents production of enzyme which degrades some hemicellulose form. The protein was produced by a genetically modified strain of E. coli in the microbiological reactor. The optimal conditions for protein biosynthesis process were indicated. The reaction rate constant was determined for the purified preparation. The enzyme stability was evaluated as a crucial operational parameter for potential application in the hydrolysis of plant biomass components in a large-tonnage process.
    Źródło:
    Inżynieria i Aparatura Chemiczna; 2015, 3; 130--132
    0368-0827
    Pojawia się w:
    Inżynieria i Aparatura Chemiczna
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Higher induction of defense enzymes and cell wall reinforcement in maize by root associated bacteria for better protection against Aspergillus niger
    Autorzy:
    Jha, Y.
    Powiązania:
    https://bibliotekanauki.pl/articles/2084643.pdf
    Data publikacji:
    2019
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    Aspergillus niger
    β-1
    3-glucanase
    biotic factor
    phenylalanine ammonia lyase
    RAPD analysis
    rhizosphere
    root associated bacteria
    Opis:
    Root associated bacteria were isolated from Suaeda nudiflora and two isolates were selected for this study: rhizospheric Bacillus megaterium and endophytic Pseudomonas aeruginosa. These isolates were inoculated into maize variety Narmada Moti during its germination. TTC (2, 3, 5-triphenyl tetrazolium chloride) staining was used to confirm the association of the isolates with the maize root. The effects of these root associated bacteria were tested alone and in combinations for cell wall reinforcement and the induction of defense enzymes such as phenylalanine ammonia lyase (PAL) and β-1,3-glucanase in the presence of fungal pathogen Aspergillus niger in maize. The results indicated that the rhizospheric bacteria had a greater fight response to fungal infection than the endophhytic bacteria due to cell wall lignification as well as the rapid induction of higher concentrations of defense related enzymes.
    Źródło:
    Journal of Plant Protection Research; 2019, 59, 3; 341-349
    1427-4345
    Pojawia się w:
    Journal of Plant Protection Research
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-5 z 5

      Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies