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Reduction of PDC1 expression in S. cerevisiae with xylose isomerase on xylose medium
Bioprocess and Biosystems Engineering, 2011Ethanol production using hemicelluloses has recently become a focus of many researchers. In order to promote D: -xylose fermentation, we cloned the bacterial xylA gene encoding for xylose isomerase with 434 amino acid residues from Agrobacterium tumefaciens, and successfully expressed it in Saccharomyces cerevisiae, a non-xylose assimilating yeast. The
Dong Min, Kim +9 more
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Streptomyces glucose/xylose isomerase has a single active site for glucose and xylose
Biochemical and Biophysical Research Communications, 1989A kinetic method which allows one to evaluate whether an enzyme acting on two different substrates has one or two active sites was employed to study the active site of glucose isomerase which catalyses the isomerization of both glucose and xylose. The experimental data on the rates of hydrolysis of mixtures of various concentrations of glucose and ...
S M, Gaikwad +3 more
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Plant selection principle based on xylose isomerase
In Vitro Cellular & Developmental Biology - Plant, 2001The xylose isomerase genes (xylA) from Thermoanaerobacterium thermosulfurogenes and Streptomyces rubiginosus were introduced and expressed in three plant species (potato, tobacco and tomato) and transgenic plants were selected on xylose-containing medium.
Haldrup, Anna +2 more
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Properties of genetically overproducedE. coli xylose isomerase
Biotechnology Letters, 1988Xylose isomerase was purified from a transformedE. coli strain (LE392-pRK248/pTXI-1) (Lastick et al., 1986) that overproduces the enzyme by induction of the strong lambda PL promotor. Kinetic data, N-terminal sequence analysis, SDS polyacrylamide gel electrophoresis, size exclusion chromatography and immunodiffusion were used to compare the ...
M. Y. Tucker +4 more
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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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A novel xylose isomerase from Neurospora crassa
Biotechnology Letters, 1996Highest production of xylose Isomerase by Neurospora crassa grown with different carbon sources was at 0.014 U mg-1 with D-xylose. The enzyme exhibited maximum activity at pH 8.0 and 70°C and retained 100% activity at 45°C for 30 min at pH 8.0. It was activated by 8 mM Mg2+ whereas 2 mM Co2+ afforded protection against inactivation by heat.
U. Rawat +3 more
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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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Xylose isomerase from Piromyces sp. E2 is a promiscuous enzyme with epimerase activity.
Enzyme and Microbial Technology, 2023M. Q. Barreto +6 more
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Catabolite repression of xylose isomerase synthesis in Arthrobacter ureafaciens
Microbiology, 2008The effect of a specific substrate as well as other carbon sources on the biosynthesis of xylose isomerase in the actinobacterium Arthrobacter ureafaciens BIM B-6 has been studied. It was established that xylose and its structural analogue xylite induced the production of the enzyme by bacterial cells.
L I, Sapunova +2 more
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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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