Chemistry: molecular biology and microbiology – Process of utilizing an enzyme or micro-organism to destroy... – Treating animal or plant material or micro-organism
Reexamination Certificate
1999-08-26
2001-02-06
Achutamurthy, Ponnathapu (Department: 1652)
Chemistry: molecular biology and microbiology
Process of utilizing an enzyme or micro-organism to destroy...
Treating animal or plant material or micro-organism
C435S196000, C435S071100
Reexamination Certificate
active
06184028
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to isolated polypeptides having pectin acetylesterase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
2. Description of the Related Art
Pectins are important structural components of plant cell walls. The main backbone in pectins can be divided into linear homogalacturonan (smooth) regions of up to 200 residues of 1,4-linked &agr;-D-galacturonic acid (GalUA) and highly branched rhamnogalacturonan (hairy) regions consisting of repeating &agr;-(1,2)-L-rhamnose-&agr;-(4)-D-galacturonic acid disaccharide units. In general, about half of the rhamnose residues are substituted with neutral oligosaccharides such as arabinans, galactans, and arabinogalactans. Most pectic substances are also esterified at some of the &agr;-D-galacturonic acid residues with methyl at the carboxyl group or acetyl at the hydroxyl groups at the C-2 and/or C-3 positions.
Pectin acetylesterase catalyzes the deacetylation of the acetyl groups at the hydroxyl groups of the linear homogalacturonan (smooth) regions. Rhamnogalacturonan acetylesterase catalyzes the deacetylation of the acetyl groups at the hydroxyl groups of the highly branched rhamnogalacturonan (hairy) regions.
Pectin acetylesterases have been isolated from
Erwinia chrysanthemi
(Shevchik et al., 1997,
Molecular Microbiology
24: 1285-1301);
Vigna radiata
L (Breton et al., 1996,
FEBS Letters
388: 139-142); and
Aspergillus niger
(Searle-Van Leeuwen et al., 1996,
Progress in Biotechnology
pp. 793-798.
A rhamnogalacturonan acetylesterase has been isolated from
Aspergillus aculeatus
(Kauppinen et al., 1995,
Journal of Biological Chemistry
270: 27172-27178; WO 93/20190).
A gene encoding pectin acetylesterase has been isolated from
Erwinia chrysanthemi
(Shevchik et al., 1997, supra).
A gene encoding rhamnogalacturonan acetylesterase has been isolated from
Aspergillus aculeatus
(Kauppinen et al., 1995, supra).
It is an object of the present invention to provide improved polypeptides having pectin acetylesterase activity and nucleic acids encoding the polypeptides.
SUMMARY OF THE INVENTION
The present invention relates to isolated polypeptides having pectin acetylesterase activity selected from the group consisting of:
(a) a polypeptide having an amino acid sequence which has at least 65% identity with amino acids 26 to 382 of SEQ ID NO:2;
(b) a polypeptide encoded by a nucleic acid sequence which hybridizes under low stringency conditions with (i) nucleotides 76 to 1146 of SEQ ID NO:1, (ii) a subsequence of (i) of at least 100 nucleotides, or (iii) a complementary strand of (i) or (ii);
(c) a variant of the polypeptide having an amino acid sequence of SEQ ID NO:2 comprising a substitution, deletion, and/or insertion of one or more amino acids;
(d) an allelic variant of (a) or (b); and
(e) a fragment of (a), (b), or (d) that has pectin acetylesterase activity.
The present invention also relates to isolated nucleic acid sequences encoding the polypeptides and to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.
REFERENCES:
patent: WO 93/20190 (1993-10-01), None
Yoshida et al. Sequencing of a 65 kb region of theBacillus subtilisgenome containing the lic and cel loci, and creation of a 177 kb contig covering the gnt-sacXY region. Microbiology (1996) 142, 3113-3123, Nov. 1996.
Kunst et al. The complete genome sequence of the gram-positive bacteriumBacillus subtilis. Nature (1997) 390 (6657): 249-256, Nov. 1997.
Shevchik et al., 1997, Molecular Microbiology 24: 1285-1301.
Breton et al., 1996, FEBS Letters 388: 139-142.
Kauppinen et al., 1995, Journal of Biological Chemistry 270: 27172-27178.
Brown Kimberly M.
Thomas Michael D.
Achutamurthy Ponnathapu
Kerr Kathleen
Lambiris Esq. Elias
Novo Nordisk Biotech Inc.
Starnes Robert
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