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glyoxylic acid/špinat
Veza se sprema u međuspremnik
8 rezultatima
The expression of spinach glycolate oxidase (GO) in E. coli and the application of GO in the production of glyoxylic acid.
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The complementary deoxyribonucleic acid (cDNA) coding spinach glycolate oxidase (GO) was amplified by reverse transcription polymerase chain reaction (RT-PCR), using the total ribonucleic acid (RNA) of spinach leaves as the template, and was cloned into cloning vector pMD18-T. After the DNA sequence
Renaturation of spinach leaf glyoxylic acid reductase.
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Sulfhydryl studies of spinach leaf glyoxylic acid reductase.
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The kinetic properties of spinach leaf glyoxylic acid reductase.
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The structural properties of spinach leaf glyoxylic acid reductase.
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High-level production of spinach glycolate oxidase in the methylotrophic yeast Pichia pastoris: engineering a biocatalyst.
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Glycolate oxidase (GO) is a flavo-enzyme that catalyzes the oxidation of glycolate, and is useful for the biocatalytic production of glyoxylate. We have produced high levels of spinach GO in the methylotrophic yeast Pichia pastoris (Pp), by chromosomal integration of multiple copies of an expression
Expression of active spinach glycolate oxidase in Aspergillus nidulans.
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The biocatalytic production of glyoxylic acid from glycolic acid requires two enzymes: glycolate oxidase, which catalyzes the oxidation of glycolic acid by oxygen to produce glyoxylic acid and hydrogen peroxide, and catalase, which decomposes the byproduct hydrogen peroxide. As an alternative to
Recombinant Hansenula polymorpha as a biocatalyst: coexpression of the spinach glycolate oxidase (GO) and the S. cerevisiae catalase T (CTT1) gene.
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The methylotrophic yeast Hansenula polymorpha has been developed as an efficient production system for heterologous proteins. The system offers the possibility to cointegrate heterologous genes in anticipated fixed copy numbers into the chromosome. As a consequence co-production of different
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