Modified xylanases exhibiting improved expression

Details Modified xylanases exhibiting improved expression Modified xylanases exhibiting improved expression

2005-03-25

2008-11-25

Prouty, Rebecca E. (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

C435S069100, C435S074000, C435S254200, C435S278000, C426S007000, C536S023200

Reexamination Certificate

active

07456005

ABSTRACT:
A modified Family 11 xylanase enzyme comprising a sequence that introduces a functional consensus glycosylation site is provided. Non-limiting examples of introduced glycosylation sites include mutation of the amino acid at position 34, 131, 180, 182, or a combination thereof, to an asparagine. The indicated amino acid position in the Family 11 xylanase is determined from sequence alignment of the xylanase of interest with that of aTrichoderma reeseixylanase II amino acid sequence. The introduced consensus glycosylation site facilitates increased expression efficiency of the modified xylanase when compared to the expression efficiency of a corresponding xylanase from which the modified xylanase was derived, using similar host strains and growth conditions.

REFERENCES:
patent: 5405769 (1995-04-01), Campbell et al.
patent: 5759840 (1998-06-01), Sung et al.
patent: 5866408 (1999-02-01), Sung et al.
patent: 6635464 (2003-10-01), Paloheimo et al.
patent: 6667170 (2003-12-01), Mantylaet et al.
patent: 2005/0208178 (2005-09-01), Bauer et al.
patent: WO 94/24270 (1994-10-01), None
patent: WO 00/29587 (2000-05-01), None
patent: WO 01/92487 (2001-12-01), None
patent: WO 02/02597 (2002-01-01), None
patent: WO 02/36752 (2002-05-01), None
patent: WO 03/046169 (2003-06-01), None
patent: WO 03/106484 (2003-12-01), None
patent: WO 03/106654 (2003-12-01), None
Arase, et al., “Stabilization of xylanase by random mutagenesis”,FEBS Lett. vol. 316, No. 2, pp. 123-127 (Jan. 1993).
Berges, et al. “Isolation of uridine auxotrophs fromTrichoderma reeseiand efficient transformation with the clonedura3 and ura5genes”Curr. Genet., vol. 19, pp. 359-365 (1991).
Berka, et al., “The development ofAspergillus nigervar.awarmorias a host for the expression and secretion of heterologous gene products,”Biochem. Soc. Trans., vol. 19: pp. 681-685 (1991).
Bissett, “A revision of the genusTrichodermaI. SectionLongibrachiatumsect. nov.,”Can. J. Bot., vol. 62, pp. 924-93 1 (1984).
Cannon, International Commission on the Taxonomy of Fungi (ICTF): name changes in fungi of microbiological, industrial and medical importance, Part 2,Microbiological Sciences, vol. 3, No. 9, (1986).
Chen, et al., “Nucleotide sequence and deduced primary structure of cellobiohydrolase II fromTrichoderma reesei,”Bio/Technology, vol. 5, pp. 274-278 (1987).
Conesa, et al., “The secretion pathway in filamentous fungi: a biotechnological view,”Fung. Genet. Biol., vol. 33, pp. 155-171 (2001).
Goldman, et al., “Transformation ofTrichoderma harzianumby high-voltage electric pulse,”Curr. Genet, vol. 17, pp. 169-174 (1990).
Gritz, et al., “Plasmid-encoded hygromycin B resistance: the sequence of hygromycin B phosphotransferase gene and its expression inEscherichia coliandSaccharomyces cerevisiae,”Genevol. 25, pp. 179-188 (1983).
Henrissat, et al., “A classification of glycosyl hydrolases based on amino acid sequence similarities,”Biochem. J., vol. 280, pp. 309-316 (1991).
Hui, et al., “Characterization of cellobiohydrolase I (Cel7A) glycoforms from extracts ofTrichoderma reeseiusing capilliary isoelectric focusing and electrospray mass spectrometry,”J. Chrom. B., vol. 752, pp. 349-368 (2001).
Hui, et al., “Indentification of glycan structure and glycosylation sites in cellobiohydrolase II and endoglucanases I and II fromTrichoderma reesei,” Glycobiology, vol. 12, No. 12, pp. 837-849 (2002).
Kuhls, et al., “Molecular evidence that the asexual industrial fungusTrichoderma reeseiis a clonal derivative of the ascomyceteHypocrea jecorina,” Proc. Natl. Acad. Sci., USA, vol. 93, pp. 7755-7760 (Jul. 1996).
Kulkarni, et al, “Molecular and biotechnical aspects of xylanases,”FEMS Microbiology Reviews, vol. 23, pp. 411-456 (1991).
Lorito, et al., “Biolistic transformation ofTrichoderma harzianumandGliocladium virensusing plasmid and genomic DNA,”Curr. Genet. vol. 24, pp. 349-356 (1993).
Luthi, “Xylanase from the Extremely Thermophilic Bacterium ‘Caldocellum saccharolyticum’: Overexpression of the Gene inEscherichia coliand Characterization of the Gene Product,”Appl. Environ. Microbiol., vol. 56, No. 9, pp. 2677-2683 (Sep. 1990).
Mandels, et al., “Induction of cellulase inTrichoderma virideas influenced by carbon sources and metals,”J. Bacteriol. vol. 73, pp. 269-278 (1956).
Montenecourt, et al., “Selective Screening Methods for the isolation of high yielding cellulase mutants ofTrichoderma reesei,” Adv. Chem. Ser.vol. 181, pp. 289-301 (1979).
Paloheimo, et al., “High-yield production of a bacterial xylanase in the filamentous fungusTrichoderma reeseirequires a carrier polypeptide with an intact domain structure,”Appl. Environ. Microbiol., vol. 69, No. 12, pp. 7073-7082 (2003).
Penttila, et al., “A versatile transformation system for the cellulolytic fungusTrichoderma reesei,” Gene, vol. 61, pp. 155-164 (1987).
Radford, et al., “Regulation of pyrimidine metabolism in Neurospora,”In Molecular Genetics of Filamentous Fungi(Timberlake, W.E., editor), Alan R. Liss (New York), pp. 127-143 (1985).
Saarelainen, et al., “Cloning, sequencing and enhanced expression of theTrichoderma reeseiendoxylanase II (pI 9),xln2,” Mol. Gen. Genet, vol. 241, pp. 497-503 (1993).
Sagt, et al., “Introduction of an N-glycosylation site increases secretion of heterologous proteins in yeasts,”Appl. Environ. Microbiol., vol. 66, No. 11, pp. 4940-4944 (Nov. 2000).
Saloheimo, et al., “The protein disulphide isomerase gene of the fungusTrichoderma reeseiis induced by endoplasmic reticulum stress and regulated by the carbon source,”Mol. Gen. Genet., vol. 262, pp. 35-45 (1999).
Shoemaker, et al., “Molecular cloning of exo-cellobiohydrolyase I derived fromTrichoderma reeseistrain L27,”Bio/Technologyvol. 1, pp. 691-696 (1983).
Simmons, et al., “Classification of Some Cellulase-Producing Trichoderma Species,”Second International Mycological Congress—Abstracts, vol. M-Z (Aug. 27-Sep. 3, 1977).
Simpson, et al., “An extremely thermostable xylanase from the termophiulic eubacteriumThermotoga,” Biochem. J., vol. 277, pp. 413-417 (1991).
Sung, et al., “Overexpression of theBacillus subtilisand circulans Xylanases inEscherichia coli,” Protein Expression Purif., vol. 4, pp. 200-206 (1993).
Te'O, et al., “Codon optimization of xylanase genexynBfrom the thermophilic bacteriumDictyoglomus thermophilumfor expression in the filamentous fungusTrichoderma reesei,” FEMS Microbiol. Letters, vol. 190, pp. 13-19 (2000).
Törrönen, et al., “The two major xylanases fromTrichoderma reesei: characterization of both enzymes and genes,”Bio/technology, vol. 10, pp. 1461-1465 (Nov. 1992).
Tsai, et al., “Retro-translocation of proteins from the endoplasmic reticulum into the cytosol,”Nature Reviews-Molecular Cell biology, vol. 3, pp. 246-255 (Apr. 2002).
Turunen, et al., “A combination of weakly stabilizing mutations with a disulfide bridge in the α-helix region ofTrichoderma resseiendo-1,4-β-xylanase II increases the thermal stability through synergism,”J. Biotech., vol. 88, pp. 37-46 (2001).
Van Den Elzen, et al., “A chimaeric hygromycin resistance gene as a selectable marker in plant cells,”Plant Mol. Biol. vol. 5, pp. 299-302 (1985).
Vanhanen, et al., “Isolation and characterization of the 3-phosphoglycerate kinase gene (pgk) from the filamentous fungusTrichoderma reesei,” Curr. Genet., vol. 15, pp. 181-186 (1989).
Vanhanen, et al., “Promoter structure and expression of the 3-phosphoglycerate kinase-encoding gene (pgkl) ofTrichoderma reesei,” Gene, vol. 106, pp. 129-133 (1991).
Vieira, et al., “Isolation of single-stranded plasmid DNA,”Methods Enzymol., vol. 153, pp. 3-11 (1987).
Winterhalter, et al., &#

Affiliated with

Also associated with

Rating

Modified xylanases exhibiting improved expression does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Modified xylanases exhibiting improved expression, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Modified xylanases exhibiting improved expression will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4021618