Phospholipases and uses thereof

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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C435S325000, C435S197000, C435S320100, C435S440000, C435S069100, C536S023200

Reexamination Certificate

active

07838274

ABSTRACT:
The invention relates to a newly identified polynucleotide sequence comprising a gene that encodes a novel phospholipase isolated fromAspergillus niger. The invention features the full length nucleotide sequence of the novel gene, the cDNA sequence comprising the full length coding sequence of the novel phospholipase as well as the amino acid sequence of the full-length functional protein and functional equivalents thereof. The invention also relates to methods of using these enzymes in industrial processes and methods of diagnosing fungal infections. Also included in the invention are cells transformed with a polynucleotide according to the invention and cells wherein a phospholipase according to the invention is genetically modified to enhance or reduce its activity and/or level of expression.

REFERENCES:
patent: 4433092 (1984-02-01), Nemeth
patent: 4567046 (1986-01-01), Inoue et al.
patent: 4631211 (1986-12-01), Houghten
patent: 4704692 (1987-11-01), Ladner
patent: 4708781 (1987-11-01), Poorten
patent: 4946778 (1990-08-01), Ladner et al.
patent: 5194392 (1993-03-01), Geysen
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5264367 (1993-11-01), Aalrust et al.
patent: 5480971 (1996-01-01), Houghten et al.
patent: 6146869 (2000-11-01), Harris et al.
patent: 2007/0207521 (2007-09-01), Albermann et al.
patent: 190264 (1981-10-01), None
patent: 0219269 (1981-09-01), None
patent: 0109244 (1987-04-01), None
patent: 0075463 (1987-05-01), None
patent: 0426211 (1993-11-01), None
patent: 0619947 (1997-04-01), None
patent: 0808903 (1997-11-01), None
patent: 0654527 (1998-01-01), None
patent: 0659344 (2001-07-01), None
patent: 60-078529 (1985-05-01), None
patent: 62-111629 (1987-05-01), None
patent: 63-258528 (1988-10-01), None
patent: 02-153997 (1990-06-01), None
patent: 10-155493 (1998-06-01), None
patent: 90/02809 (1990-03-01), None
patent: 91/17271 (1991-11-01), None
patent: 92/01047 (1992-01-01), None
patent: 92/09690 (1992-06-01), None
patent: 92/15679 (1992-09-01), None
patent: 92/18619 (1992-10-01), None
patent: 92/20791 (1992-11-01), None
patent: 93/01288 (1993-01-01), None
patent: 95/00636 (1995-01-01), None
patent: 98/26057 (1998-06-01), None
patent: 98/45453 (1998-10-01), None
patent: 00/32758 (2000-06-01), None
patent: 01/11974 (2001-02-01), None
patent: 02/26044 (2002-04-01), None
patent: 02/49441 (2002-06-01), None
Berka et al. “Aspergillus orizaeEST SEQ ID No. 4754” EMBL Database accession No. AAF12231 (Sep. 2000).
Chakravarti et al. “Studies on phospholipase activities inNeurospora crassaconidia” Arch. Biochem. Biophys. 206:393-402 (1981).
Chen et al. “Identification of extracellular phospholipase B, lysophospholipase, and acyltransferase produced byCryptococcus neoformans” Infec. Immun. 65:405-411 (1997).
Chica et al. “Semi-rational approaches to engineering enzyme activity: Combining the benefits of directed evolution and rational design” Curr. Opn. Biotechnol. 16:378-384 (2005).
Fifis et al. “Evidence for phospholipase B activity inFusobacterium necrophorumcultures and its association with hemolysin/leucocidin activities” Vet. Microbiol. 49:219-233 (1996).
Ichimasa et al. Purification and some properties of soluble phospholipase B from baker's yeast (Saccharomyces cerevisiae) Agric. Biol. Chem. 49:1083-1089 (1985).
Kawasaki et al. “Studies on a phospholipase B fromPenicillium notatum. Purification, properties, and mode of action” J. Biochem. 77:1233-1244 (1975).
Kuwabara et al. “Purification and some properties of water-soluble phospholipase B fromTorulaspora delbrueckir” Agric. Biol. Chem. 52:2451-2458 (1988).
Lee et al. “TheSaccharomyces cerevisiaePLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity” J. Biol. Chem. 269:19725-19730 (1994).
Machida et al. “Aspergillus oryzaepolynucleotide SEQ ID No. 5401” EMBL Database accession No. ABZ56288 (Oct. 2002).
Masuda et al. “Primary structure of protein moiety ofPenicillium notatumphospholipase B deduced from the cDNA” Eur. J. Biochem. 202:783-787 (1991).
Mustranta et al. “Comparison of lipases and phospholipases in the hydrolysis of phospholipids” Process Biochem. 30:393-401 (1995).
Saito et al. “Phospholipase B fromPenicillium notatum” Meth. Enzymol. 197:446-456 (1991).
Seffernick et al. “Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionality different” J. Bacteriol. 183:2405-2410 (2001).
Tseung et al. “Production of phosphatidases by phytopathogens” Phytopathol. Notes 58:1437-1438 (1968).
Uehara et al. “Purification and properties of phospholipase A1produced byCorticium centrifugum” Agric. Biol. Chem. 43:517-525 (1979).
Watanabe et al. “Cloning and sequencing of phospholipase B gene from the yeastTorulaspora delbrueckir”FEMS Microbiol. Lett. 124:29-34 (1994).
Witkowski et al. “Conversion of a β-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine” Biochem. 38:11643-11650 (1999).
International Search Report for PCT/EP2003/05450 completed Aug. 13, 2003.
International Preliminary Examination Report for PCT/EP2003/05450 completed Oct. 28, 2004.

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