Alcohol oxidase
Alcohol oxidase structure
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Common Name | Alcohol oxidase | ||
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| CAS Number | 9073-63-6 | Molecular Weight | 191.311 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C2H5NO2.2[C4H10] | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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[Effect of nitrogen source on gene expression of first steps of methanol utilization pathway in Pichia pastoris].
Genetika 49(4) , 454-60, (2013) Pichia pastoris is a methylotrophic yeast that is widely used for the expression of heterologous proteins. Here, we have investigated the dependence of AOX1 and CAT1 expression on the source of nitrogen. It has shown that the expression of AOX1 and CAT1 depen... |
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Heterologous protein expression in Pichia thermomethanolica BCC16875, a thermotolerant methylotrophic yeast and characterization of N-linked glycosylation in secreted protein.
FEMS Microbiol. Lett. 334(2) , 127-34, (2012) This study describes Pichia thermomethanolica BCC16875, a new methylotrophic yeast host for heterologous expression. Both methanol-inducible alcohol oxidase (AOX1) and constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoters from Pichia pastoris ... |
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Improvement of porcine interferon-α production by recombinant Pichia pastoris via induction at low methanol concentration and low temperature.
Appl. Biochem. Biotechnol. 165(2) , 559-71, (2011) Improved porcine interferon-α (pIFN-α) production by recombinant Pichia pastoris was achieved by culture conditions optimization in a 5-l bioreactor. The results indicated that the pIFN-α concentration, specific methanol consumption rate, specific activities ... |
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Multimeric immobilization of alcohol oxidase on electrospun fibers for valid tests of alcoholic saliva.
J. Biotechnol. 168(1) , 46-54, (2013) An accurate quantitation of ethanol is of great importance in clinical and forensic analyses. In the current study, alcohol oxidase (AOX) from Pichia pastoris, a multimeric enzyme consisting of eight identical subunits, was immobilized on electrospun polystyr... |
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Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003.
Curr. Microbiol. 34(6) , 374-7, (1997) Alcohol oxidase from Candida methanosorbosa was purified about sixfold with a yield of 37.6% from the culture broth of Candida methanosorbosa M-2003. The enzyme preparation was homogeneous on slab gel electrophoresis. The purified enzyme had an optimal pH fro... |
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Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases.
Biochemistry. (Mosc.) 77(8) , 843-56, (2012) This review considers quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases, enzymes that are present in numerous methylotrophic eu- and prokaryotes and significantly differ in their primary and quaternary structure. The cofactors of the... |
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Alcohol oxidase, a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyethylene glycol.
Biochim. Biophys. Acta 151(2) , 330-42, (1968)
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Expression of lignocellulolytic enzymes in Pichia pastoris.
Microb. Cell Fact. 11 , 61, (2012) Sustainable utilization of plant biomass as renewable source for fuels and chemical building blocks requires a complex mixture of diverse enzymes, including hydrolases which comprise the largest class of lignocellulolytic enzymes. These enzymes need to be ava... |
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Cloning, sequencing and expression analysis of a gene encoding alcohol oxidase in Paenibacillus sp. AIU 311.
J. Biosci. Bioeng. 110(2) , 147-51, (2010) We have cloned a gene encoding an alcohol oxidase (AOD) specific to aldehyde alcohols from Paenibacillus sp. AIU 311. The AOD gene contains an open reading frame consisting of 618 nucleotides corresponding to 205 amino acid residues. The deduced amino acid se... |
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Molecular characterization of the fatty alcohol oxidation pathway for wax-ester mobilization in germinated jojoba seeds.
Plant Physiol. 161(1) , 72-80, (2013) Jojoba (Simmondsia chinensis) is the only plant species known to use liquid wax esters (WEs) as a primary seed storage reserve. Upon germination, WE hydrolysis releases very-long-chain fatty alcohols, which must be oxidized to fatty acids by the sequential ac... |