Polypeptides having glucoamylase activity

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

Reexamination Certificate

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C435S252300, C435S252330, C435S320100, C536S023200

Reexamination Certificate

active

06921656

ABSTRACT:
Polypeptides having the amino acid sequence represented by SEQ ID NO:6 in Sequence Listing or an amino acid sequence derived from the above sequence by at least one of deletion, addition, insertion or substitution of one or more amino acids and showing a thermophilic glucoamylase activity.

REFERENCES:
patent: 0 648 843 (1995-04-01), None
patent: WO 90/11352 (1990-10-01), None
Maeder et al. (Aug. 1999) Genetics, vol. 152(4), pp. 1299-1305.
Weiss (Feb. 25, 2002) GenBank accession AE010170.
Laderman et al., “α-Amylase from the Hyperthermophilic ArchaebacteriumPyrococcus furiosus”, The Journal of Biological Chemistry, (1993), vol. 268, No. 32, pp. 24402-24407.
Lawson et al., “Nucleotide Sequence and X-ray Structure of Cyclodextrin Glycosyltransferase fromBacillus circulansStrains 251 in a Maltose-dependent Crystal Form”,Journal of Molecular Biology, (1994), vol. 236, pp. 590-600.
Jørgensen et al., Cloning, Sequencing, Characterization, and Expression of an Extracellular α-Amylase from the Hyperthermophilic ArchaeonPyrococcus furiosus, inEscherichia coliandBacillus subtilis, Journal of Biological Chemistry, (1997), vol. 272, No. 26, pp. 16335-16342.
Costantino et al., “Purification and Characterization of an α-Glucosidase from a Hypertermophilic Archaebacterium,Pyrococcus furiosus, Exhibiting a Temperature Optimum of 105 to 115°C”,Journal of Bacteriology, (1990), vol. 172, No. 7, pp. 3654-3660.
Bauer et al., “An Endoglucanase, Eg1A, from the Hyperthermophilic ArchaeonPyrococcus furiosus, Hydrolyzes β-1,4 Bonds in Mixed-Linkage (1→3), (1→4)-β-D-Glucans and Cellulose”,Journal of Bacteriology, (1999), vol. 181, No. 1, pp. 284-290.
Voorhorst et al., Characterization of the celB Gene Coding for β-Glucosidase from the Hyperthermophilic ArchaeonPyrococcus furiosusand Its Expression and Site-Directed Mutation inEscherichia coli, Journal of Bacteriology, vol. 177, No. 24, pp. 7105-7111.
B. Costanzo et al; “Starch-hydrolyzing enzymes from thermophilic archaea and bacteria”,Current Opinion in Chemical Biology, vol. 6, No. 2, pp. 151-160, Apr. 2002.
Dong et al; “Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase fromPyrococcus furiosusand biochemical characterization of the recombinant enzyme”;Applied and Environmental Microbiology, vol. 63, No. 9, pp. 3569-3576; Sep. 1997.
K. Laderman et al; “The purification and Characterization of an Extremely Thermostable alpha-amylase from the hyperthermophilic archaebacteriumPyrococcus furiosus”; Journal of Biological Chemistry, American Society of Biological Chemists; vol. 268, No. 32, pp. 24394-24401, Nov. 1993.

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