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1966
Publisher Summary This chpater discusses the determination of D-xylose isomerase. The assay method commonly used is based on the determination of the xylulose formed in the reaction by cysteine–carbazole test. One unit is defined as the amount of enzyme required to produce one micromole of D-xylulose in 10 minutes of incubation.
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Publisher Summary This chpater discusses the determination of D-xylose isomerase. The assay method commonly used is based on the determination of the xylulose formed in the reaction by cysteine–carbazole test. One unit is defined as the amount of enzyme required to produce one micromole of D-xylulose in 10 minutes of incubation.
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Exploring the interaction between D-xylose isomerase and D-xylose by free energy calculation
Proteins: Structure, Function, and Genetics, 1996The numerical quadrature thermodynamic integration method is used to investigate enzyme-substrate interaction of D-xylose isomerase. A screening function for the coulombic interaction is introduced into the simulation to correct the effect of finite cut-off radius for the non-bonded interaction.
H, Hu, Y Y, Shi, C X, Wang
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Molecular Simulations of Solute Transport in Xylose Isomerase Crystals
The Journal of Physical Chemistry B, 2008Cross-linked enzyme crystals (CLECs) enclose an extensive regular matrix of chiral solvent-filled nanopores, via which ions and solutes travel in and out. Several cross-linked enzyme crystals have recently been used for chiral separation and as biocatalysts. We studied the dynamics of solute transport in orthorhombic d-xylose isomerase (XI) crystals by
Kourosh, Malek, Marc-Olivier, Coppens
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A Plate Method to Screen for Microorganisms Producing Xylose Isomerase
Microbiology, 2004A plate method was developed to screen for xylose isomerase-producing microorganisms based on the use of 2,3,5-triphenyltetrazolium as an indicator of D-xylulose, the D-xylose isomerization product. The use of this method allows microorganisms to be differentiated by the character of the enzyme synthesis (inducible or constitutive).
L I, Sapunova +3 more
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Biological Chemistry Hoppe-Seyler, 1990
The D-xylose isomerase from T. aquaticus accepts, besides D-xylose, also D-glucose, and, with lower efficiency, D-ribose, and D-arabinose as alternative substrates. The activity of the enzyme is strictly dependent on divalent cations. Mn2+ is most effective in the D-xylose isomerase reaction and Co2+ in the D-glucose isomerization.
A, Lehmacher, H, Bisswanger
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The D-xylose isomerase from T. aquaticus accepts, besides D-xylose, also D-glucose, and, with lower efficiency, D-ribose, and D-arabinose as alternative substrates. The activity of the enzyme is strictly dependent on divalent cations. Mn2+ is most effective in the D-xylose isomerase reaction and Co2+ in the D-glucose isomerization.
A, Lehmacher, H, Bisswanger
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Inhibition of d-xylose isomerase by pentitols and d-lyxose
Archives of Biochemistry and Biophysics, 1969Abstract The inhibition of crystalline d -xylose isomerase from Lactobacillus brevis by pentitols and carbohydrate derivatives has been examined. Of the pentitols, xylitol and l - and d -arabitol inhibited competitively, whereas ribitol was ineffective. The inhibition constants ( K i ) are: 0.0027, 0.13, or 0.146 m for xylitol, d -arabitol,
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Paradigm shift in xylose isomerase usage: a novel scenario with distinct applications
Critical Reviews in Biotechnology, 2022Renan Yuji Miyamoto +2 more
exaly
Xylose isomerase from Piromyces sp. E2 is a promiscuous enzyme with epimerase activity
Enzyme and Microbial Technology, 2023Adriana Grandis +2 more
exaly
Journal of the American Chemical Society, 1953
Rolf M. Hochster, R. Wade Watson
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Rolf M. Hochster, R. Wade Watson
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