Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
molecular biology
-
Pichia pastoris is an efficient host for the expression and secretion of heterologous proteins possessing a strong and tightly regulated promoter from the alcohol oxidase I, AOX1, gene. The transformed cells need to be activated by methanol and grow on methanol as carbon source. With the inducible AOX1 promoter an increase of the copy number above two resulted in a decrease of expression. Combined use of GAP and AOX1 promoters in Pichia pastoris, overview
analysis
-
enzyme may be useful for the colorimetric determination of methanol, ethanol, or other alcohols
analysis
-
the enzyme is useful for construction of ethanol biosensors
analysis
-
a dual biosensor analysis system based on alcohol oxidase and alcohol dehydrogenase for the simultaneous analysis of methanolethanol mixtures is developed. The alcohol dehydrogenase biosensor quantifies only the ethanol in the range 0.3-8 mmol/l without interference from methanol in concentrations as high as 100 mmol/l. The alcohol oxidase biosensor is able to respond to both analytes in the range 3-70 mmol/l for methanol and 15110 mmol/l for ethanol. The concentration of ethanol and methanol from the sample is determined by processing analytical signals obtained from both biosensors
analysis
-
amperometric sensor for ethanol based on one-step electropolymerization of thionine-carbon nanofiber nanocomposite containing alcohol oxidase. The ethanol biosensor can monitor ethanol ranging from 0.002 to 0.252 mM with a detection limit of 0.0017 mM. It displays a rapid response, an expanded linear response range as well as excellent reproducibility and stability
analysis
-
an amperometric biosensor for ethanol monitoring is developed and optimised. The biosensor uses poly(neutral red), as redox mediator, which is electropolymerised on carbon film electrodes and alcohol oxidase from Hansenula polymorpha as recognition element, immobilised by cross-linking with glutaraldehyde in the presence of bovine serum albumin as carrier protein. The biosensor is used for the determination of ethanol in Portuguese red and white wines. No significant interferences were found from compounds usually present in wine
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
AOD gene and isozyme structure may be used as a basis for reclassification of the methylotrophic yeasts
analysis
-
selection procedure for isolation of the mutant forms of AOX, and their use as a suitable bioelement for biosensor technologies. The created biosensor based on mAOX (from the strain CA2) was characterised by a decreased affinity towards analyzed substrates and slightly increased Vmax. The operational stability of the mAOX-immobilised electrode is not affected and remains similar to an electrode based on the natural enzyme. The described methodology opens up the possibility for construction of biosensors appropriate for precise, rapid, and cheap analysis of target analytes, e.g. ethanol in real samples of wines, beers or fermentation cultures
analysis
-
the enzyme is useful in alcohol biosensor applications
analysis
-
fabrication of a self-powered ethanol biosensor comprising a beta-NAD+-dependent alcohol dehydrogenase bioanode and a bienzymatic alcohol oxidase and horseradish peroxidase biocathode. beta-NAD+ is regenerated by means of a toluidine blue modified redox polymer. The biofuel cell exhibits an open-circuit voltage of approximately 660 mV and can be used as self-powered device for the determination of the ethanol content in liquor
analysis
-
the behaviour of commercially available AOx and ADH enzymes is studied in 12 different biosensor designs towards butanol-1 detection in liquid media. Four out of twelve proposed designs demonstrate a good signal reproducibility and linear response (up to 14.6 mM of butanol) under very low applied potentials (from -0.02 to -0.32 V)
biotechnology
in the core promoter and 5' untranslated region of the gene, mutations in the TATA box motif, regions downstream of the transcription start site or next to the start codon in the 5' UTR have a significant effect on expression. Mutations in most other regions are tolerated. These neutral core promoter positions, not affecting expression, can be exploited to introduce extrinsic sequence elements such as cloning sites and bacterial promoters
biotechnology
-
in the core promoter and 5' untranslated region of the gene, mutations in the TATA box motif, regions downstream of the transcription start site or next to the start codon in the 5' UTR have a significant effect on expression. Mutations in most other regions are tolerated. These neutral core promoter positions, not affecting expression, can be exploited to introduce extrinsic sequence elements such as cloning sites and bacterial promoters
-
degradation
-
the purified enzyme is able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 0.04 nm/ml concentration
degradation
-
the purified enzyme is able to decolorize textile dyes, Red HE7B (57.5%) and Direct Blue GLL (51.09%) within 15 h at 0.04 nm/ml concentration
-
synthesis
-
enantioselective oxidation of thioanisole with a bienzymatic couple alcohol oxidase/peroxidase
synthesis
-
expression of alcohol dehydrogenase with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D). The resulting bifunctional biocatalysts retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidases, while merely requiring a catalytic amount of NADP+
synthesis
-
expression of alcohol dehydrogenase with a thermostable NADPH-oxidase fusion partner (phenylacetone monooxygenase C65D). The resulting bifunctional biocatalysts retains the catalytic properties of the individual enzymes, and acts essentially like alcohol oxidases, while merely requiring a catalytic amount of NADP+
synthesis
the combination of alcohol oxidase and catalase is most effective in converting over 97% 5-hydroxymethylfurfural to 2,5-diformylfuran in 72 h
synthesis
when covalently immobilized onto barium ferrite (BaFe12O19) magnetic microparticles, an immobilization efficiency of 71.0 % and catalytic activity of 34.6 U/g can be obtained. The immobilized OthAOX works optimally at 55°C and pH 8.0. More than 65% of the initial immobilized enzyme activity is retained after 24 h pre-incubation at 45°C. The immobilized enzyme shows a greater catalytic efficiency for oxidation of methanol and ethanol than free enzyme and can be recovered by magnetization and recycled for at least three consecutive batches, after which 70% activity remains
synthesis
-
the combination of alcohol oxidase and catalase is most effective in converting over 97% 5-hydroxymethylfurfural to 2,5-diformylfuran in 72 h
-