Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.37 extracted from

  • Guerfali, M.; Maalej, I.; Gargouri, A.; Belghith, H.
    Catalytic properties of the immobilized Talaromyces thermophilus beta-xylosidase and its use for xylose and xylooligosaccharides production (2009), J. Mol. Catal. B, 57, 242-249.
No PubMed abstract available
Search for more literature for 3.2.1.37

Application

Application Comment Organism
synthesis immobilization of enzyme on chitosan as best support material gives immobilization and activity yields of 94% and 87%, respectively, of initial activity, and also provides the highest stability, retaining 94% of its initial activity even after being recycled 25times. Maximal activity of immobilized enzyme is achieved at pH 8.0 and 53°C, whereas that for the free enzyme is obtained at pH 7.0 and 50°C. The immobilized enzyme is more thermostable than the free beta-xylosidase. Km values of the free enzyme increases from 2.37 mM to 3.42 mM at the immobilized state. Immobilized enzyme catalyzes the reverse hydrolysis reaction, forming xylooligosaccharides in the presence of a high concentration of xylose. Co-immobilized of beta-xylosidase and xylanase on chitosan leads to a continuous hydrolysis of 3% oat spelt xylan at 50°C and better hydrolysis yields and higher amount of xylose are obtained Thermomyces dupontii

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 5 mM, 70% residual activity of native enzyme, 96% of immobilized enzyme Thermomyces dupontii
EDTA 5 mM, 55% residual activity of native enzyme, 63% of immobilized enzyme Thermomyces dupontii
Fe2+ 5 mM, 20% residual activity of native enzyme, 42% of immobilized enzyme Thermomyces dupontii
Hg2+ 5 mM, 49% residual activity of native enzyme, 64% of immobilized enzyme Thermomyces dupontii
SDS 5 mM, 44% residual activity of native enzyme, 65% of immobilized enzyme Thermomyces dupontii
Zn2+ 5 mM, 34% residual activity of native enzyme, 56% of immobilized enzyme Thermomyces dupontii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.37
-
 4-nitrophenyl-beta-D-xylopyranoside native enzyme, pH 7.0, 50°C Thermomyces dupontii
3.42
-
 4-nitrophenyl-beta-D-xylopyranoside immobilized enzyme, pH 7.0, 50°C Thermomyces dupontii

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 5 mM, 45% stimulation of native enzyme, 20% of immobilized enzyme Thermomyces dupontii
Co2+ 5 mM, 22% stimulation of native enzyme, 11% of immobilized enzyme Thermomyces dupontii
Mn2+ 5 mM, 30% stimulation of native enzyme, 28% of immobilized enzyme Thermomyces dupontii

Organism

Organism UniProt Comment Textmining
Thermomyces dupontii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 D-xylose
-
 Thermomyces dupontii xylobiose + H2O and higher xylooligosaccharides, immobilized enzyme in presence of high concentration of xylose r
4-nitrophenyl beta-D-xylopyranoside + H2O
-
 Thermomyces dupontii 4-nitrophenol + beta-D-xylose
-
 ?