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Wyszukujesz frazę "3-glucanase" wg kryterium: Temat


Wyświetlanie 1-2 z 2
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:
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
    Wyświetlanie 1-2 z 2

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