Construction of methylotrophic yeast Hansenula polymorpha strains over-producing formaldehyde dehydrogenase
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چکیده
منابع مشابه
Bioconversion of airborne formaldehyde by immobilized formaldehyde dehydrogenase from the recombinant methylotrophic yeast Hansenula polymorpha
Formaldehyde (FA) is a very toxic pollutant. FA in indoor air has a negative effect on human health and should be removed by ventilation or by conversion to non-toxic products. The formaldehyde dehydrogenase (FdDH), a NADand glutathione-dependent enzyme from recombinant methylotrophic yeast Hansenula polymorpha, was tested for its ability to oxidize airborne FA. A continuous fluidized bed biore...
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BACKGROUND Currently, the two most commonly used fibrinolytic agents in thrombolytic therapy are recombinant tissue plasminogen activator (rt-PA) and streptokinase (SK). Whereas SK has the advantage of substantially lower costs when compared to other agents, it is less effective than either rt-PA or related variants, has significant allergenic potential, lacks fibrin selectivity and causes tran...
متن کاملBiosynthesis of peroxisomal enzymes in the methylotrophic yeast Hansenula polymorpha.
The dramatic expansion of the peroxisomal compartment known to occur in the methanol-utilizing yeast Hansenula polymorpha on transfer from glucose- to methanol-containing media was shown to be accompanied by the synthesis of at least six major polypeptides that dominate the polypeptide pattern of total cell extracts analyzed by NaDodSO(4)/polyacrylamide gel electrophoresis. Two of these polypep...
متن کاملHARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization.
The HARO7 gene of the methylotrophic, thermotolerant yeast Hansenula polymorpha was cloned by functional complementation. HARO7 encodes a monofunctional 280-amino-acid protein with chorismate mutase (EC 5.4. 99.5) activity that catalyzes the conversion of chorismate to prephenate, a key step in the biosynthesis of aromatic amino acids. The HARO7 gene product shows strong similarities to primary...
متن کاملA novel platform for the production of nonhydroxylated gelatins based on the methylotrophic yeast Hansenula polymorpha.
The use of yeast as a host for heterologous expression of proteins that are normally derived from animal tissue is a promising way to ensure defined products that are devoid of potential harmful animal side products. Here we report on the production and secretion of a custom-designed gelatin, Hu3-His8, by the yeast Hansenula polymorpha. We observed that Hu3-His8 was poorly secreted by the heter...
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ژورنال
عنوان ژورنال: Biopolymers and Cell
سال: 2005
ISSN: 0233-7657,1993-6842
DOI: 10.7124/bc.000710