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11. Engineering of geranylgeranyl pyrophosphate synthase levels and physiological conditions for enhanced carotenoid and astaxanthin synthesis in

Author

Breitenbach, Jürgen, Visser, Hans, Verdoes, Jan C., Ooyen, Albert J. J., Sandmann, Gerhard, Molecular Biosciences 213, Goethe-Universität Frankfurt am Main, Section of Fungal Genomics, Wageningen University and Research [Wageningen] (WUR), Dyadic Netherlands, and Division of Industrial Microbiology

Subjects
Light enhancement, food and beverages, Carotenoid biosynthesis, 3-hydroxy-4-keto-torulene, Geranylgeranyl pyrophosphate synthase
Abstract

International audience; The basidiomycetous yeast, is one of the very few organisms which can be used for biological production of the carotenoid astaxanthin. cDNA has been cloned from this fungus for engineering of the terpenoid pathway. The function of its gene product as a geranylgeranyl pyrophosphate synthase was established. was transformed with the cDNA to divert metabolite flow from the sterol pathway towards carotenoid biosynthesis. Transformants were obtained with increased levels of geranylgeranyl pyrophosphate synthase leading to higher carotenoid levels including astaxanthin. Physiological conditions for maximum carotenoid synthesis for wild type and the CrtE transformant were dim light and extra air supply of the shaking culture. These conditions and the transformation with had additive effects and resulted in an 8-fold higher astaxanthin formation as compared to the initial wild type culture without illumination and extra air supply yielding 451 μg/g dry wt within 4 days of growth.

Published
2010
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12. Genes involved in carotene synthesis and mating in Blakeslea trispora

Author

Poulsen, Vera Kuzina, Ramírez-Medina, Humberto, Visser, Hans, Ooyen, Albert J. J. van, Cerdá-Olmedo, Enrique, Berg, Johan A. van der, Poulsen, Vera Kuzina, Ramírez-Medina, Humberto, Visser, Hans, Ooyen, Albert J. J. van, Cerdá-Olmedo, Enrique, and Berg, Johan A. van der

Published
2008

13. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Author

Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, Stam, Hein, Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, and Stam, Hein

Abstract

The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid. We sequenced the 33.9-megabase genome of A. niger CBS 513.88, the ancestor of currently used enzyme production strains. A high level of synteny was observed with other aspergilli sequenced. Strong function predictions were made for 6,506 of the 14,165 open reading frames identified. A detailed description of the components of the protein secretion pathway was made and striking differences in the hydrolytic enzyme spectra of aspergilli were observed. A reconstructed metabolic network comprising 1,069 unique reactions illustrates the versatile metabolism of A. niger. Noteworthy is the large number of major facilitator superfamily transporters and fungal zinc binuclear cluster transcription factors, and the presence of putative gene clusters for fumonisin and ochratoxin A synthesis.

Published
2007

14. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Author

Sub Molecular Microbiology, Molecular Microbiology, Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, Stam, Hein, Sub Molecular Microbiology, Molecular Microbiology, Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, and Stam, Hein

Published
2007

17. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Author

Pel, Herman J, primary, de Winde, Johannes H, additional, Archer, David B, additional, Dyer, Paul S, additional, Hofmann, Gerald, additional, Schaap, Peter J, additional, Turner, Geoffrey, additional, de Vries, Ronald P, additional, Albang, Richard, additional, Albermann, Kaj, additional, Andersen, Mikael R, additional, Bendtsen, Jannick D, additional, Benen, Jacques A E, additional, van den Berg, Marco, additional, Breestraat, Stefaan, additional, Caddick, Mark X, additional, Contreras, Roland, additional, Cornell, Michael, additional, Coutinho, Pedro M, additional, Danchin, Etienne G J, additional, Debets, Alfons J M, additional, Dekker, Peter, additional, van Dijck, Piet W M, additional, van Dijk, Alard, additional, Dijkhuizen, Lubbert, additional, Driessen, Arnold J M, additional, d'Enfert, Christophe, additional, Geysens, Steven, additional, Goosen, Coenie, additional, Groot, Gert S P, additional, de Groot, Piet W J, additional, Guillemette, Thomas, additional, Henrissat, Bernard, additional, Herweijer, Marga, additional, van den Hombergh, Johannes P T W, additional, van den Hondel, Cees A M J J, additional, van der Heijden, Rene T J M, additional, van der Kaaij, Rachel M, additional, Klis, Frans M, additional, Kools, Harrie J, additional, Kubicek, Christian P, additional, van Kuyk, Patricia A, additional, Lauber, Jürgen, additional, Lu, Xin, additional, van der Maarel, Marc J E C, additional, Meulenberg, Rogier, additional, Menke, Hildegard, additional, Mortimer, Martin A, additional, Nielsen, Jens, additional, Oliver, Stephen G, additional, Olsthoorn, Maurien, additional, Pal, Karoly, additional, van Peij, Noël N M E, additional, Ram, Arthur F J, additional, Rinas, Ursula, additional, Roubos, Johannes A, additional, Sagt, Cees M J, additional, Schmoll, Monika, additional, Sun, Jibin, additional, Ussery, David, additional, Varga, Janos, additional, Vervecken, Wouter, additional, van de Vondervoort, Peter J J, additional, Wedler, Holger, additional, Wösten, Han A B, additional, Zeng, An-Ping, additional, van Ooyen, Albert J J, additional, Visser, Jaap, additional, and Stam, Hein, additional

Published
2007
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27. Heterologous protein production in the yeast Kluyveromyces lactis.

Author

Van Ooyen, Albert J. J., Dekker, Peter, Huang, Michael, Olsthoorn, Maurien M. A., Jacobs, Denise I., Colussi, Paul A., and Taron, Christopher H.

Subjects
*KLUYVEROMYCES marxianus, *BIOTECHNOLOGY, *SACCHAROMYCES, *YEAST, *FOOD industry
Abstract

Kluyveromyces lactis is both scientifically and biotechnologically one of the most important non- Saccharomyces yeasts. Its biotechnological significance builds on its history of safe use in the food industry and its well-known ability to produce enzymes like lactase and bovine chymosin on an industrial scale. In this article, we review the various strains, genetic techniques and molecular tools currently available for the use of K. lactis as a host for protein expression. Additionally, we present data illustrating the recent use of proteomics studies to identify cellular bottlenecks that impede heterologous protein expression. [ABSTRACT FROM AUTHOR]

Published
2006
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28. Kluyveromyces as a Host for Heterologous Gene Expression: Expression and Secretion of Prochymosin

Author

van den Berg, Johan A., primary, van der Laken, Kees J., additional, van Ooyen, Albert J. J., additional, Renniers, Ton C. H. M., additional, Rietveld, Krijn, additional, Schaap, Albert, additional, Brake, Anthony J., additional, Bishop, Robert J., additional, Schultz, Kathleen, additional, Moyer, Donna, additional, Richman, Michael, additional, and Shuster, Jeffrey R., additional

Published
1990
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29. Codon usage in Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma).

Author

Verdoes, Jan C. and van Ooyen, Albert J. J.

Subjects
PROTEINS, BIOMOLECULES, AMINO acids, HOMOLOGY (Biology), CRYPTOGAMS, NUCLEOTIDE sequence
Abstract

By sequence analysis of 96 randomly selected clones in a cDNA library of Xanthophyllomyces dendrorhous, ten novel, full-length clones encoding cytoplasmic ribosomal proteins (rp) were found. The deduced amino acid sequences showed significant homology to their counterparts from eukaryotic origin including mammals, fungi and plants. Some ribosmal protein encoding cDNAs appeared several times, but by Southern blot analysis it was shown they are encoded by a single copy gene. The nucleotide sequences of ten full length cDNAs were used to investigate the codon usage in X. dendrorhous. [ABSTRACT FROM AUTHOR]

Published
2000
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31. Cloning and characterization of the astaxanthin biosynthetic gene encoding phytoene desaturase of <TOGGLE>Xanthophyllomyces dendrorhous</TOGGLE>

Author

Verdoes, Jan C., Misawa, Norihiko, and Ooyen, Albert J. J. van

Abstract

The first carotenoid biosynthetic gene from the basidiomycetous yeast Xanthophyllomyces dendrorhous was isolated by heterologous complementation in Escherichia coli. The isolated gene, denominated as crtI, was found to encode for phytoene desaturase. The coding region is interrupted by 11 introns. The deduced amino acid sequence showed significant homology with its bacterial and eukaryotic counterparts, especially those of fungal origin. A plasmid containing the geranylgeranyl diphosphate synthase and phytoene synthase encoding genes from Erwinia uredovora was introduced in E. coli together with the phytoene desaturase encoding cDNA from X. dendrorhous. As a result, lycopene accumulation was observed in these transformants. We conclude that in X. dendrorhous the four desaturase steps, by which phytoene is converted into lycopene, are carried out by a single gene product. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 63: 750–755, 1999.

Published
1999
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32. Phytase-containing Transgenic Seeds as a Novel Feed Additive for Improved Phosphorus Utilization

Author

Pen, Jan, Verwoerd, Theo C., van Paridon, Peter A., Beudeker, Rob F., van den Elzen, Peter J. M., Geerse, Kees, van der Klis, Jan D., Versteegh, Hans A. J., van Ooyen, Albert J. J., and Hoekema, André

Abstract

Phytate is the main storage form of phosphorus in many plant seeds, but bound in this form it is a poor nutrient for monogastric animals. Its availability can be significantly increased by addition of the enzyme phytase, which releases phosphate from the substrate, phytate. We have engineered a phytase from Aspergillus niger in tobacco seeds, providing a stable and convenient packaging of the enzyme that is directly applicable in animal feed. The enzyme was expressed as 1 percent of the soluble protein in mature seeds. In in vitro tests that simulated chicken crop and stomach conditions, release of phosphate from feed by addition of transgenic seeds was demonstrated. Supplementation of broiler diets with transgenic seeds resulted in an unproved growth rate, comparable to diets supplemented with fungal phytase or phosphorus. Addition of phytase-transgenic seeds to animal feed thus obviates the need for inorganic phosphorus supplementation, and is environmentally desirable because of the reduced excretion of phosphorus.

Published
1993
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33. Production of Active Bacillus licheniformis Alpha-Amylase in Tobacco and its Application in Starch Liquefaction

Author

Pen, Jan, Molendijk, Lucy, Quax, Wim J., Sijmons, Peter C., van Ooyen, Albert J. J., van den Elzen, Peter J. M., Rietveld, Krijn, and Hoekema, André

Abstract

As a first example of the feasibility of producing industrial bulk enzymes in plants, we have expressed Bacillus licheniformis α-amylase in transgenic tobacco, and applied the seeds directly in starch liquification. The enzyme was properly secreted into the intercellular space, and maximum expression levels of about 0.3% of total soluble protein were obtained. No apparent effect of the presence of the enzyme on plant phenotype was observed. The molecular weight of the enzyme produced in tobacco was around 64 kD. The difference, compared to 55.2 kD for the bacterial enzyme, was found to result from complex-type carbohydrate chains attached to the protein. Application studies on the liquefaction of starch were done with transgenic seeds containing the re-combinant α-amylase. The resulting hydrolysis products were virtually identical with those obtained from degradation with α-amylase from Bacillus licheniformis.

Published
1992
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34. Kluyveromyces as a Host for Heterologous Gene Expression: Expression and Secretion of Prochymosin

Author

van den Berg, Johan A., van der Laken, Kees J., van Ooyen, Albert J. J., Renniers, Ton C. H. M., Rietveld, Krijn, Schaap, Albert, Brake, Anthony J., Bishop, Robert J., Schultz, Kathleen, Moyer, Donna, Richman, Michael, and Shuster, Jeffrey R.

Abstract

We have developed the yeast Kluyveromyces lactis as a host organism for the production of the milk-clotting enzyme chymosin. In contrast to Saccharomyces cerevisiae, we found that this yeast is capable of the synthesis and secretion of fully active prochymosin. Various signal sequences could be used to efficiently direct the secretion of prochymosin in Kluyveromyces, but not in S. cerevisiae. We conclude that the efficient synthetic and secretory capacity of this heterologous protein is a property of the yeast Kluyveromyces. These results have led to the development of a large scale production process for chymosin.

Published
1990
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37. Specific inhibition of ribosomal RNA synthesis in vitroby guanosine 3′ diphosphate, 5′ diphosphate

Author

VAN OOYEN, ALBERT J. J., DE BOER, HERMAN A., AB, GEERT, and GRUBER, MAX

Abstract

CONSIBERABLE evidence has accumulated that guanosine 3′-diphosphate, 5′-diphosphate (ppGpp)1is involved in the regulation of ribosomal RNA (rRNA) synthesis in Escherichia coli in vivo(see ref. 2). The involvement of ppGpp is most convincingly indicated by results obtained under conditions of amino acid starvation. A strong increase in ppGpp accumulation is always accompanied by a concomitant decrease in stable RNA accumulation3. In vitro, a specific effect of ppGpp has not been found, neither in a purified4, nor in a crude system5. Travers et al.6,7have proposed that ppGpp specifically affects rRNA synthesis by counteracting the effects of the protein elongation factor EF-Tu. Here, we show that ppGpp can specifically inhibit rRNA synthesis in vitrousing purified RNA polymerase with two templates—DNA prepared by phenol extraction, and nucleoids prepared using methods developed by Pettijohn et al.8.

Published
1975
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38. Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015 versus enzyme-producing CBS 513.88.

Author

Andersen MR, Salazar MP, Schaap PJ, van de Vondervoort PJ, Culley D, Thykaer J, Frisvad JC, Nielsen KF, Albang R, Albermann K, Berka RM, Braus GH, Braus-Stromeyer SA, Corrochano LM, Dai Z, van Dijck PW, Hofmann G, Lasure LL, Magnuson JK, Menke H, Meijer M, Meijer SL, Nielsen JB, Nielsen ML, van Ooyen AJ, Pel HJ, Poulsen L, Samson RA, Stam H, Tsang A, van den Brink JM, Atkins A, Aerts A, Shapiro H, Pangilinan J, Salamov A, Lou Y, Lindquist E, Lucas S, Grimwood J, Grigoriev IV, Kubicek CP, Martinez D, van Peij NN, Roubos JA, Nielsen J, and Baker SE

Subjects
Base Sequence, Gene Expression Profiling, Gene Rearrangement genetics, Gene Transfer, Horizontal genetics, Genomics methods, Molecular Sequence Data, Polymorphism, Single Nucleotide genetics, Sequence Analysis, DNA, Species Specificity, Synteny genetics, Aspergillus niger genetics, Computational Biology methods, Evolution, Molecular, Genetic Variation, Genome, Fungal genetics, Phylogeny
Abstract

The filamentous fungus Aspergillus niger exhibits great diversity in its phenotype. It is found globally, both as marine and terrestrial strains, produces both organic acids and hydrolytic enzymes in high amounts, and some isolates exhibit pathogenicity. Although the genome of an industrial enzyme-producing A. niger strain (CBS 513.88) has already been sequenced, the versatility and diversity of this species compel additional exploration. We therefore undertook whole-genome sequencing of the acidogenic A. niger wild-type strain (ATCC 1015) and produced a genome sequence of very high quality. Only 15 gaps are present in the sequence, and half the telomeric regions have been elucidated. Moreover, sequence information from ATCC 1015 was used to improve the genome sequence of CBS 513.88. Chromosome-level comparisons uncovered several genome rearrangements, deletions, a clear case of strain-specific horizontal gene transfer, and identification of 0.8 Mb of novel sequence. Single nucleotide polymorphisms per kilobase (SNPs/kb) between the two strains were found to be exceptionally high (average: 7.8, maximum: 160 SNPs/kb). High variation within the species was confirmed with exo-metabolite profiling and phylogenetics. Detailed lists of alleles were generated, and genotypic differences were observed to accumulate in metabolic pathways essential to acid production and protein synthesis. A transcriptome analysis supported up-regulation of genes associated with biosynthesis of amino acids that are abundant in glucoamylase A, tRNA-synthases, and protein transporters in the protein producing CBS 513.88 strain. Our results and data sets from this integrative systems biology analysis resulted in a snapshot of fungal evolution and will support further optimization of cell factories based on filamentous fungi.

Published
2011
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39. Metabolic engineering of the astaxanthin-biosynthetic pathway of Xanthophyllomyces dendrorhous.

Author

Visser H, van Ooyen AJ, and Verdoes JC

Subjects
Basidiomycota genetics, Gene Expression Regulation, Fungal, Recombinant Proteins genetics, Recombinant Proteins metabolism, Xanthophylls, beta Carotene genetics, Basidiomycota metabolism, Genetic Engineering methods, beta Carotene analogs & derivatives, beta Carotene biosynthesis
Abstract

This review describes the different approaches that have been used to manipulate and improve carotenoid production in Xanthophyllomyces dendrorhous. The red yeast X. dendrorhous (formerly known as Phaffia rhodozyma) is one of the microbiological production systems for natural astaxanthin. Astaxanthin is applied in food and feed industry and can be used as a nutraceutical because of its strong antioxidant properties. However, the production levels of astaxanthin in wild-type isolates are rather low. To increase the astaxanthin content in X. dendrorhous, cultivation protocols have been optimized and astaxanthin-hyperproducing mutants have been obtained by screening of classically mutagenized X. dendrorhous strains. The knowledge about the regulation of carotenogenesis in X. dendrorhous is still limited in comparison to that in other carotenogenic fungi. The X. dendrorhous carotenogenic genes have been cloned and a X. dendrorhous transformation system has been developed. These tools allowed the directed genetic modification of the astaxanthin pathway in X. dendrorhous. The crtYB gene, encoding the bifunctional enzyme phytoene synthase/lycopene cyclase, was inactivated by insertion of a vector by single and double cross-over events, indicating that it is possible to generate specific carotenoid-biosynthetic mutants. Additionally, overexpression of crtYB resulted in the accumulation of beta-carotene and echinone, which indicates that the oxygenation reactions are rate-limiting in these recombinant strains. Furthermore, overexpression of the phytoene desaturase-encoding gene (crtI) showed an increase in monocyclic carotenoids such as torulene and HDCO (3-hydroxy-3',4'-didehydro-beta,-psi-carotene-4-one) and a decrease in bicyclic carotenoids such as echinone, beta-carotene and astaxanthin.

Published
2003
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