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Hansenula polymorpha

Traditional and well-established yeast species are Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Pichia pastoris and Schizosaccharomyces pombe. With every year that passes they are increasingly being used in industrial and pharmaceutical enzyme production on a large scale. Many further yeasts present interesting features (e.g. Arxula adeninivorans and Yarrowia lipolytica), but are not that widely used. [Pg.45]

Steinborn, G., Boer, E., Scholz, A. et al. (2006) Application of a wide-range yeast vector (CoMed) system to recombinant protein production in dimorphic Arxula adeninivorans, methylotrophic Hansenula polymorpha and other yeasts. Microbial Cell Factories, 5, 33. [Pg.53]

Gellissen, G., Kunze, G., Gaillardin, C. et al. (2005) New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolytica - a comparison. FEMS Yeast Research, 5 (11), 1079-1096. [Pg.56]

The yeast Hansenula polymorpha serves as the production system for a recombinant hepatitis B vaccine (Berna Biotech AG [8] and yeast is also used to produce granulocyte-macrophage colony stimulating factor (GM-CSF), marketed as Leukine by Schering AG. [Pg.268]

Handylab, 26 976 Hanford N reactor, 17 572-573 Hanford production reactors, 17 570 Hanksite, 5 785t Hansa yellows, 14 317 Hansch equation, 10 329 Hansenula polymorpha, 12 479 Hantaviruses, 3 137 Hantzsch pyridine synthesis, 16 550 Hantzsch-Widman nomenclature system, 17 399... [Pg.418]

Welford R. W. D. Lam A. Mirica L. M. Klinman J. P. Partial conversion of Hansenula polymorpha amine oxidase into a plant amine oxidase implications for copper chemistry and mechanism. Biochemistry 2007, 46, 10817-10827. [Pg.456]

Mills S. A. Goto Y. SuQ. Plastino J. Klinman J. P. Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha. Biochemistry 2002, 41, 10577-10584. [Pg.456]

Takahashi K. Klinman J. P. Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits. Biochemistry 2006, 45, 4683 1694. [Pg.456]

The polysaccharide from Hansenula polymorpha 52-251 has a block type of structure of the main chain, with (1— -2)- and (1— 6)-linked a-D-mannopyranosyl units. The side chains also contain (l- 2) links interspersed with (1— 6) links. Immunochemical experiments revealed the presence of a-D-glucopyranosyl phosphate determinants,118 in common with the polysaccharide of Hansenula wingei, a yeast of interest because of its sexual, agglutination factors.104... [Pg.87]

In an alternate process, enantioselective microbial reduction of 6-oxobus-pirone (19, Fig. 18.6) to either (R)- and (.S )-6-hydroxybuspirone was described. About 150 microorganisms were screened for the enantioselective reduction of 19. Rhizopus stolonifer SC 13898, Rhizopus stolonifer SC 16199, Neuros-pora crassa SC 13816, Mucor racemosus SC 16198, and Pseudomonas putida SC 13817 gave >50% reaction yields and >95% ee s of (,S )-6-hydroxybuspi-rone. The yeast strains Hansenula polymorpha SC 13845 and Candida maltosa SC 16112 gave (R)-6-hydroxybuspirone in >60% reaction yield and >97% ee (Patel et aL, 2005). [Pg.327]

Bruinenberg, P. G., Evers, M., Waterham, H. R., Kuipers, J., and Amberg, A. C., 1989, Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha, Biochem. Biophys. Acta, 1008 157iil67. [Pg.224]

Plastino, J., Green, E. L., Sanders-Loehr, J., and Klinman, J. P., 1999, An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha. Biochemistry, 820488216D. [Pg.228]

Leao-Helder, A.N., Krikken, A.M., Van der Klei, I.J., Kiel, J.A. and Veenhuis, M. (2003) Transcriptional down-regulation of peroxisome numbers affects selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 278, 40749 0756. [Pg.259]

Yeasts Easy to grow in large-scale volumes Able to glycosylate. Improved glycosylating yeast Pichiapastorisand Hansenula polymorpha Easy to achieve secretion of recombinant proteins into growth medium Gene expression can be difficult to control Some post-translational modifications may not be correct... [Pg.428]


See other pages where Hansenula polymorpha is mentioned: [Pg.462]    [Pg.347]    [Pg.92]    [Pg.142]    [Pg.241]    [Pg.23]    [Pg.129]    [Pg.127]    [Pg.618]    [Pg.522]    [Pg.257]    [Pg.72]    [Pg.462]    [Pg.88]    [Pg.200]    [Pg.223]    [Pg.525]    [Pg.579]    [Pg.447]    [Pg.165]    [Pg.163]    [Pg.276]    [Pg.327]    [Pg.328]    [Pg.328]    [Pg.203]    [Pg.5811]    [Pg.254]    [Pg.642]    [Pg.124]    [Pg.186]   
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