Polypeptide

Details Polypeptide Polypeptide

2006-12-08

2010-12-28

Ramirez, Delia M (Department: 1652)

Chemistry: molecular biology and microbiology

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

Hydrolase

C435S200000, C435S204000, C435S069100

Reexamination Certificate

active

07858352

ABSTRACT:
We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

REFERENCES:
patent: 4683202 (1987-07-01), Mullis
patent: 4946779 (1990-08-01), Kameda et al.
patent: 5204254 (1993-04-01), Schmid et al.
patent: 5958749 (1999-09-01), Kubota et al.
patent: 5989169 (1999-11-01), Svendsen et al.
patent: 6162628 (2000-12-01), Cherry et al.
patent: 6242224 (2001-06-01), Nakano et al.
patent: 6667065 (2003-12-01), Kragh et al.
patent: 7166453 (2007-01-01), Kragh et al.
patent: 7371552 (2008-05-01), Kragh et al.
patent: 2003/0134395 (2003-07-01), Shetty et al.
patent: 2005/0059131 (2005-03-01), Bisgard-Frantzen et al.
patent: 2005/0112237 (2005-05-01), Kragh et al.
patent: 2005/0136524 (2005-06-01), Kragh et al.
patent: 2005/0137111 (2005-06-01), Kragh et al.
patent: 2006/0008888 (2006-01-01), Kragh et al.
patent: 2006/0008890 (2006-01-01), Kragh et al.
patent: 2006/0018997 (2006-01-01), Kragh et al.
patent: 2006/0073583 (2006-04-01), Kragh et al.
patent: 2007/0020727 (2007-01-01), Berg et al.
patent: 2007/0020731 (2007-01-01), Kragh et al.
patent: 2007/0072270 (2007-03-01), Kragh et al.
patent: 2007/0141693 (2007-06-01), Berg et al.
patent: 2008/0107773 (2008-05-01), Kragh et al.
patent: 2008/0227173 (2008-09-01), Berg et al.
patent: 2008/0274531 (2008-11-01), Berg et al.
patent: 2008/0292747 (2008-11-01), Berg et al.
patent: 120 693 (1984-03-01), None
patent: 0 298 645 (1989-11-01), None
patent: 0 412 607 (1991-02-01), None
patent: 0 494 233 (1991-04-01), None
patent: 6-279745 (1994-10-01), None
patent: 6-279746 (1994-10-01), None
patent: WO 91/04669 (1991-04-01), None
patent: WO 99/23211 (1999-05-01), None
patent: WO 99/50399 (1999-10-01), None
patent: WO 00/58447 (2000-10-01), None
patent: WO 02/068589 (2002-09-01), None
patent: WO 2004/111217 (2004-12-01), None
patent: WO 2005/003339 (2005-01-01), None
patent: WO 2005/007818 (2005-01-01), None
patent: WO 2005/007867 (2005-01-01), None
patent: WO 2006/003461 (2006-01-01), None
Zhou, J. et al, “Nucleotide sequence of the maltotetraohydrolase gene fromPseudomonas saccharophila,” FEBS Letters, vol. 255, 1989, pp. 37-41.
Fogarty, W., 1983, Microbial Amylases, W.M. Fogarty (Ed.) Microbial enzymes and biotechnology, Applied Science, London, pp. 1-92.
Fogarty, W. et al, “Starch-Degrading Enzymes of Microbial Origin,” M.J. Bull (Ed.), Progress in Industrial Microbiology, vol. 15, Elsevier Scientific, 1979, pp. 87-150.
Kainuma, K. et al, “Isolation and action pattern of maltohexaose producing amylase fromaerobacter aerogenes,” FEBS Letters, vol. 26, No. 1, Oct. 1972, pp. 281-285.
U.S. Appl. No. 11/887,977, filed Oct. 5, 2007, Berg et al.
U.S. Appl. No. 12/339,718, filed Dec. 19, 2008, Derkx et al.
Yoshiyuki Takasaki, “Production of Maltohexaose by α-Amylase fromBacillus circulansG-6”, Agric. Biol. Chem., vol. 46, No. 6, 1982, pp. 1539-1547.
Hajime Taniguchi et al., “Purification ofBaccillus circulansF-2 Amylase and Its General Properties”, Agric. Biol. Chem. vol. 47, No. 3, 1983, pp. 511-519.
Francis J. Bealin-Kelly et al., “The α-amylase of the caldoactive bacteriumBacillus caldovelox”, Biochemical Society Transactions, vol. 18, No. 2, 1990, pp. 310-311.
William M. Fogarty et al., “A novel maltohexaose-forming α-amylase fromBacillus caldovelox: patterns and mechanisms of action”, Appl Microbiol Biotechnol, 1991, vol. 36, pp. 184-189.
Narimasa Saito, “A Thermophilic Extracellular α-Amylase fromBaccilus licheniformis”, Archives of Biochemistry and Biophysics, vol. 155, 1973, pp. 290-298.
Hisashi Okemoto et al., “Isolation and cultivation of a novel microorganism producing a maltopentaose-forming enzyme”, Appl Microbiol Biotechnol, 1986, vol. 25, pp. 137-142.
Hajime Taniguchi “Matohexaose-Producing Amylase ofBacillus circulansF-2” National Food Research Institute, 1991, pp. 111-124.
Altschul et al., 1990, J. Mol. Biol. 403-410. “Basic Local Alignment Search Tool”.
PCT/US2004/021723, Jun. 21, 2007, International Search Report.
Beucage S.L. et al., (1981)Tetrahedron Letters22, p. 1859-1869. “Deoxynucleoside Phosphoramidites-A New Class of Key Intermediates for Deoxypolynucleotide Synthesis”.
Devereux et al., 1984, Nuc. Acids Research 12 p. 387. “A Comprehensive set of sequence analysis programs for the VAX”.
Henrissat B, Bairoch A; Biochem. J., 316,695-696 (1996)) “Updating the sequence-based classification of glycosyl hydrolases.”
Matthes et al., (1984)EMBO J. 3, p. 801-805 “Simultaneous rapid chemical synthesis of over one hundred oligonucleotides on a microscale”.
Saiki R K et al. (Science(1988) 239, pp. 487-491. “Primer-Directed Enzymatic Amplification of DNA with a Thennostable DNA polymerase”.
Yoshiyuki Sakano et al., “Purification and Properties of an exo-α-Amylase fromPseudomonas stutzer”, Agric. Biol. Chem., vol. 46, No. 3, 1982, pp. 639-646.
Yoshiyuki Takasaki et al., “Maltotetraose-producing Amylase fromBacillussp. MG-4”, Agric. Biol. Chem., vol. 55, No. 7, 1991, pp. 1715-1720.
Geneseq Database Accession No. ADW75735, A. Gernot, et al., Stutzeri Maltotetrahydrolase Mature Protein Seq ID 7, Apr. 7, 2005.
Geneseq Database Accession No. ADW73063, C. T. Berg, et al., Stutzeri Maltotetrahydrolase Protein Seq ID12, Apr. 7, 2005.
Geneseq Database Accession No. ADW75733, A. Gernot, et al., Saccharophilia Variant Maltotetrahydrolase Protein Seq ID 5, Apr. 7, 2005.
A.K. Chandra et al., “Production of Extracellular Thermostable α-Amylase byBacillus licheniformis”, J. Ferment. Technol. vol. 58, No. 1, 1980, pp. 1-10.
R.A.K. Srivastava et al., “Culture Conditions for Production of Thermostable Amylase byBacillus stearothermophilus”, Applied and Environmental Microbiology, Jul. 1986, pp. 179-184.
Veronique Planchot et al.., “Purification and characterization of extracellular alpha-amylase fromAspergillus fumigatus”, Carbohydrate Research, vol. 272, 1995, pp. 97-109.
Ohnishi et al., “General Consideration for Conditions and Methods of Amylase Assay”, Handbook of Amylases and Related Enzymes, The Amylase Research Society of Japan, 1988, pp. 10-14.
Kim L. Larsen et al., “Purification and characterization of cyclodextrin glycosyltransferase fromPaenibacillussp. F8”, Carbohydrate Research, vol. 310, 1998, pp. 211-219.
Helmut Blum et al., “Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels”, Electrophoresis, 1987, vol. 8, pp. 93-99.
Hidetsugu Fuwa, “A New Method for Microdetermination of Amylase Activity by the Use of Amylose as the Substrate”, The Journal of Biochemistry, vol. 41, No. 5, 1954, pp. 583-603.
Akira Tsukamoto et al, “Nucleotide Sequence of the Maltohexaose-Producing Amylase Gene from an AlkalophilicBacillussp. #707 and Structural Similarity to Liquefying Type α-Amylase”, Biochemical and Biophysical Research Communications, vol. 151, No. 1, Feb. 29, 1988, pp. 25-31.
Y.C. Lee, “Carbohydrate analyses with high-performance anion-exchange chromatography”, Journal of Chromatography A., vol. 720, 1996, pp. 137-149.
Robert N. Ammeraal et al., “High-performance anion-exchange chromatography with pulsed amperometric detection of linear and branched glucose oligosaccharides”, Carbohydrate Research, vol. 215, 1991, pp. 179-192.
Greg Winter et al., “Man-made antibodies”, Nature, vo

Affiliated with

Also associated with

Rating

Polypeptide does not yet have a rating. At this time, there are no reviews or comments for this patent.

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

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4152372