Results 151 to 160 of about 10,917 (195)
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Determination of the anomeric configuration of D-xylose with D-xylose isomerases

Carbohydrate Research, 1976
Abstract The anomeric configuration of D -xylose, resulting from hydrolysis of β- D xylopyranosides by β- D -xylosidase from Bacillus pumilus , has been determined by an enzymic procedure, based on the stereospecificity of D -xylose isomerases. The initial hydrolysis product is α- D -xylose.
H, Kersters-Hilderson   +3 more
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Overproduction of E. coli xylose isomerase

Biotechnology Letters, 1986
A promoterles DNA fragment containing theE. coli xylose isomerase gene and its ribosome binding site was ligated into a plasmid downstream from the strong λ PL promoter. The plasmid was then used to transformE. coli strains containing a temperature-sensitive λ repressor (cI857).
S. M. Lastick   +3 more
openaire   +1 more source

Crystallographic studies of the mechanism of xylose isomerase

Biochemistry, 1989
The mechanism of xylose isomerase (EC 5.3.1.5) has been studied with X-ray crystallography. Four refined crystal structures are reported at 3-A resolution: native enzyme, enzyme + glucose, enzyme + glucose + Mg2+, and enzyme + glucose + Mn2+. One of these structures (E.G.Mg) was determined in a crystal mounted in a flow cell.
G K, Farber   +4 more
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Reduction of PDC1 expression in S. cerevisiae with xylose isomerase on xylose medium

Bioprocess and Biosystems Engineering, 2011
Ethanol 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, 1989
A 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, 2001
The 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
openaire   +1 more source

Properties of genetically overproducedE. coli xylose isomerase

Biotechnology Letters, 1988
Xylose 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
openaire   +1 more source

[104] d-Xylose isomerase

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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A novel xylose isomerase from Neurospora crassa

Biotechnology Letters, 1996
Highest 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, 1996
The 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
openaire   +2 more sources

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