Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Lyase
Reexamination Certificate
2009-07-08
2011-11-29
Swope, Sheridan (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Lyase
Reexamination Certificate
active
08067222
ABSTRACT:
The invention is directed to polypeptides having pectate lyase (pectinase) activity, polynucleotides encoding the polypeptides, and methods for making and using these polynucleotides and polypeptides. The polypeptides of the invention can be used as pectate lyases to catalyze the beta-elimination or hydrolysis of pectin and/or polygalacturonic acid, such as 1,4-linked alpha-D-galacturonic acid. The invention provides methods of treating fibers, fabrics or any pectate- or polygalacturonic acid-comprising material using one or more pectate lyases of the invention.
REFERENCES:
patent: 4788066 (1988-11-01), Witt
patent: 5582681 (1996-12-01), Back et al.
patent: 5605793 (1997-02-01), Stemmer
patent: 5709796 (1998-01-01), Fuqua et al.
patent: 5830696 (1998-11-01), Short
patent: 5912407 (1999-06-01), Miller et al.
patent: 5939250 (1999-08-01), Short
patent: 5980581 (1999-11-01), Patterson et al.
patent: 6017751 (2000-01-01), von der Osten et al.
patent: 6021536 (2000-02-01), Wasinger et al.
patent: 6024766 (2000-02-01), Wasinger
patent: 6066233 (2000-05-01), Olsen et al.
patent: 6077316 (2000-06-01), Lund et al.
patent: 6162260 (2000-12-01), Liu et al.
patent: 6187580 (2001-02-01), Andersen et al.
patent: 6197070 (2001-03-01), Horner et al.
patent: 6221406 (2001-04-01), Meschonat et al.
patent: 6241849 (2001-06-01), Franks
patent: 6258590 (2001-07-01), Lange et al.
patent: 6261828 (2001-07-01), Lund
patent: 6264925 (2001-07-01), Fuglsang et al.
patent: 6309871 (2001-10-01), Outtrup et al.
patent: 6329333 (2001-12-01), Merz et al.
patent: 6333301 (2001-12-01), Kamiya et al.
patent: 6365561 (2002-04-01), Vinson et al.
patent: 6368843 (2002-04-01), Andersen et al.
patent: 6399351 (2002-06-01), Bjornvad et al.
patent: 6399561 (2002-06-01), Schneider et al.
patent: 6410064 (2002-06-01), Akazawa
patent: 6429000 (2002-08-01), Andersen et al.
patent: 6551358 (2003-04-01), Miller et al.
patent: 2002/0115194 (2002-08-01), Lange et al.
patent: 2002/0142438 (2002-10-01), Andersen et al.
patent: 2003/0040454 (2003-02-01), Cuperus et al.
patent: 2004/0034888 (2004-02-01), Liu et al.
patent: 0552728 (1993-07-01), None
patent: WO 95/14807 (1995-06-01), None
patent: WO 97/01629 (1997-01-01), None
patent: WO 98/24965 (1998-06-01), None
patent: WO 00/26464 (2000-05-01), None
patent: WO 01/79440 (2001-10-01), None
patent: WO 02/081815 (2002-10-01), None
patent: WO 02/092741 (2002-11-01), None
patent: WO 03/002705 (2003-01-01), None
patent: WO 03/002810 (2003-01-01), None
NiceZyme view of Enzyme: EC 4.2.2.2. Downloaded Jun. 20, 2011.
Al-Hooti, Chemical composition and quality of date syrup as affected by pectinase/cellulase enzyme treatment,Food Chemistry, 2002, 79:215-220.
Bartling, “Synergism betweenErwiniapectate lyase isoenzymes that depolymerize both pectate and pectin”,Microbiology, 1995, 141:873-881.
Essa, et. al., “Effect of macerate enzymes on the yield, quality, volatile compounds and rheological property of prickly pear juice”,Nahrung/Food, 2002, 46(4):245-250.
Essa, “Effect of pectinase enzyme treatment on the rheological, physical and chemical properties of plum, banana and guava juices”,Polish Journal of Food and Nutrition Sciences, 2002, 11(3):13-19.
Hoondal, et. al., “Microbial alkaline pectinases and their industrial applications: a review”,Applied Microbiology and Biotechnology, 2002, 59:409-418.
Hurlbert, et. al., “Differences in the solution structures of the parallel β-helical pectate lyases as determined by limited proteolysis”,Biochimica et Biophysica Acta, 2002, 1599(1-2):9-20.
Angayarkanni, et. al., “Improvement of Tea Leaves Fermentation withAspergillusssp. Pectinase”,Journal of Bioscience and Bioengineering, 2002, 94(4):299-303.
Malathi, et. al., In Vitro Evaluation of Nonstarch Polysaccharide Digestibility of Feed Ingredients by Enzymes,Poultry Science, 2001, 80(3):302-305.
Nasuno, et. al., “Polygalacturonase ofErwinia carotovra”, J. Biol. Chem., 1966, 241:5298-5306.
Revilla, et. al., “Addition of pectolytic enzymes: an enological practice which improves the chromaticity and stability of red wines”,International Journal of Food Science&Technology, 2003, 38(1):29-36.
Tamaru, et. al., “Pectate lyase A, an enzymatic subunit of theClostridium cellolovoranscellulosome”,PNAS, 2001, 98(7):4125-4129.
Nelson, et al., “Pectate Lyase,” NCBI Database AAD35518, Jun. 1, 1999.
Brown, et al., Pectate Lyase 10A, fromPseudomonas cellulosais a modular enzyme containing a family 2a carbohydrate-binding molecule,Biochem J., 2001, 355:155-165.
NiceZyme view of Enzyme: EC 4.2.2.2 Downloaded Feb. 15, 2008.
Galye et al. Identification of regions in interleukin-1 alpha important for activity. J. Biol. Chem. Oct. 15, 1993; 268(29):22105-11.
Whisstock et al, Prediction of protein function from protein sequence and structure Q Rev Biophys Aug. 2003; 36(3):307-40. Review.
Carthew et al., Gene silencing by double-stranded RNA. Curr. Opin. Cell Biol. Apr. 2001; 13(2):24408. Review.
Takao, et. Al., “Molecular cloning, DNA sequence, and expression of the gene encoding for thremostable pectate lyase of thermophilicBacillussp. TS 47”, Bioscience Biotechnology and Biochemistry, 2001, 65(2):322-329.
Kluskens, et. al., “Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacteriumThermotoga maritima.”, Biochem J., 2003, 370(2):615-659.
EMBL Database AE012106, May 28, 2002.
UNIPROT Database Q8A515, Jun. 1, 2003.
EMBL Database AF279264, Nov. 5, 2000.
UNIPROT Database Q9F7L3—9GAMM, Mar. 1, 2001.
EMBL Database AB062880, Apr. 23, 2002.
UNIPROT Database Q8RR73—9BACI, Jun. 1, 2002.
EST database Accession No. G128381 van der Hoeven et al Jan. 31, 2001. Alignment with SID 1.
USPTO in house alignment of SEQ ID No. 78 with GenBank Accession No. AAG29353 from Brown et al, Biochem J. Apr. 1, 2001; 355(Pt 1):155-65.
USPTO in house alignment of SEQ ID No. 132 with GenBank Accession No. AAG29353, residues 327-649, from Biochem J. Apr. 1, 2001; 355(Pt 1):155-65.
EPO—Dec. 28, 2006—EP Supplementary Partial Search Report—EP04758802.5.
EMBL Accession No. ADY07053—Polypeptide Sequence—(2005).
EPO—Mar. 15, 2007—EP Supplementary Search Report—EP04758802.5.
EPO—Jan. 22, 2009—94(3) Communication—EP04758802.5.
CIPO—Jan. 27, 2011—Office Action (Requisition)—CA2521402.
UNIPROT Database Accession No. Q9F7L3—Charnock—(2001).
EPO—May 9, 2011—Extended EP Search Report—EP10180846.7.
UNIPROT Database Accession No. Q59420—Hugovieux-Cotte-Pattat—(1996).
EMBL Database Accession No. AJ132325—Hugovieux-Cotte-Pattat—(1999).
Dahod Samun
Gerendash Joel
Gray Kevin
Janssen Giselle
Kerovuo Janne
Linkowski Lynn M.
Siddons Brian W.
Swope Sheridan
Verenium Corporation
Verenium Corporation
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