Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2007-04-17
2007-04-17
Saidha, Tekchand (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C536S023200, C435S091500
Reexamination Certificate
active
11347886
ABSTRACT:
The present invention relates to a granular starch hydrolyzing enzyme composition comprising an acid stable alpha amylase (asAA) having granular starch hydrolyzing activity. The invention also relates to a one-step method for producing an alcohol which comprises contacting a granular starch substrate with an acid-stable alpha amylase (asAA) having granular starch hydrolyzing (GSH) activity and a glucoamylase (GA) in a fermentation step which also comprises ethanologenic microorganisms at a temperature of 25–40° C. to obtain a fermentation broth having 5 to 20% ethanol.
REFERENCES:
patent: 4092434 (1978-05-01), Yoshizumi et al.
patent: 4316956 (1982-02-01), Lutzen
patent: 4460687 (1984-07-01), Ehnstrom
patent: 4514496 (1985-04-01), Yoshizumi et al.
patent: RE32153 (1986-05-01), Tamura et al.
patent: 4587215 (1986-05-01), Hirsh
patent: 4618579 (1986-10-01), Dwiggins et al.
patent: 4727026 (1988-02-01), Sawada et al.
patent: 4863864 (1989-09-01), Ashikari et al.
patent: 5028539 (1991-07-01), Ingram et al.
patent: 5246853 (1993-09-01), Clarkson et al.
patent: 5424202 (1995-06-01), Ingram et al.
patent: 5475101 (1995-12-01), Ward et al.
patent: 5482846 (1996-01-01), Ingram et al.
patent: 5487989 (1996-01-01), Fowler et al.
patent: 5514583 (1996-05-01), Picataggio et al.
patent: 5554520 (1996-09-01), Fowler et al.
patent: 5650322 (1997-07-01), Clarkson et al.
patent: 5874276 (1999-02-01), Fowler et al.
patent: 6022725 (2000-02-01), Fowler et al.
patent: 6268328 (2001-07-01), Mitchinson et al.
patent: 0 171218 (1993-10-01), None
patent: 0 244234 (2001-11-01), None
patent: 0 215594 (2003-10-01), None
patent: WO 92/00381 (1992-01-01), None
patent: WO 92/06209 (1992-04-01), None
patent: WO 99/28488 (1999-07-01), None
patent: WO 00/04136 (2000-01-01), None
patent: WO 02/38787 (2002-05-01), None
patent: WO 02/074895 (2002-09-01), None
patent: WO 03/066826 (2003-08-01), None
patent: WO 03/068976 (2003-08-01), None
patent: WO 04/080923 (2004-09-01), None
patent: WO 04/113551 (2004-12-01), None
patent: WO 05/069840 (2005-08-01), None
Sequence search alignment between Applicants' SEQ ID No. 3 and Accession No. Q13296.
Alexopoulos, C. J. (1962)Introductory Mycology, Wiley, New York—Book Not Sent.
Allison, Daniel S. et al., “Transformation of the thermophilic fungusHumicola griseavar.thermoideaand overproduction ofHumicolaglucoamylase,” Current Genetics, vol. 21, pp. 225-229, 1992.
Altshul, Stephen F. et al., “Gapped Blast and PSI-Blast : a new generation of protein database search programs,” Nucleic Acids Research, vol. 25, No. 17, pp. 3389-3402, 1997.
Arasaratnam et al., “Synergistic Action of α-Amylase and Gluco-amylase on Raw Corn,”starch/starke, 45 (1993) Nr. 6, S. 231-233.
Ashikari, Toshihiko et al., “RhizopusRaw-Starch-Degrading Glucoamylase : Its Cloning and Expression in Yeast,” Agric. Biol. Chem., vol. 50, No. 4, pp. 957-964, 1986.
Ausubel et al., Eds., Current Protocols in Molecular Biology, 1987, Supplement 30, section 7.7.18 Book Not Sent.
Ausubel et al., Eds., Current Protocols in Molecular Biology, 1994, Book Not Sent.
Bennett, J. W. et al., ed.,More Gene Manipulations in Fungi, Academic Press, San Diego, pp. 70-77, 1991.
Bergquist, Peter, et al. “Expression of xylanase enzymes from thermophilic microorganisms in fungal hosts”,Extremophiles, V6/3, Jun. 6, 2002, pp. 177-184.
Bhikhabhai, Ramagauri et al., “Isolation of Celluloytic Enzymes fromTrichoderma reesei, QM 9414,” Journal of Applied Biochemistry, vol. 6, pp. 336-345, 1984.
Boel, E. et al., “Glucoamylases G1 and G2 fromAspergillus nigerare synthesized from two different but closely related mRNAs,” The EMBO Journal, vol. 3, No. 5, pp. 1097-1102, 1984.
Boel, E. et al., “Two different types of intervening sequences in the glucoamylase gene fromAspergillus niger,” The EMBO Journal, vol. 3, No. 7, pp. 1581-1585, 1984.
Brown, S. W. and Oliver, S. G., “The Effect of Temperature on the Ethanol Tolerance of the Yeast,”Biotechnology Letters, 4:269-274 (1982).
Brumbauer, Aniko et al., Fractionation of cellulase and β-glucosidase in aTrichoderma reesei, Bioseparation, vol. 7, pp. 287-295, 1999.
Campbell, Edward I. et al., Improved transformation efficiency ofAspergillus niger, Current Genetics, vol. 16, pp. 53-56, 1989.
Cao, Qing-Na et al., “Penicillopepsin-JT2, a recombinant enzyme fromPenicillium janthinellumand the contribution of a hydrogen bond in subsiteS3tokcat,” Protein Science, vol. 9, pp. 991-1001, 2000.
Casey, G. P. and Ingledew, W. M., “Reevaluation of Alcohol Synthesis and Tolerance in Brewer's Yeast,”Journal of the American Society of Brewing Chemists, Inc. 43(2):75-83 (1985).
Chen, Frank Y. et al., “Regulation of mammalian ribonucleotide reductase R1 mRNA stability is mediated by a ribonucleotide reductase R1 mRNA 3-untranslated region cis-trans interaction through a protein kinase C-controlled pathway,” Biochem. J., vol. 302, pp. 125-132, 1994.
Chen, Hsiu-mei et al., “Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production ofAspergillus awamoriglucoamylase,” Protein Engineering, vol. 9, No. 6, pp. 499-505, 1996.
Chen, Hsiu-mei et al., “Identification and elimination by site-directed mutagenesis of thermolabile aspartyl bonds inAspergillus awamoriglucoamylase,” Protein Engineering, vol. 8, No. 6, pp. 575-582, 1995.
Cheng, C. et al., “Efficient production of taka-amylase A by trichoderma Viride”,Agricultural and Biological Chemistry,Japan Soc. For Bioscience, Biotechnology and Agrochem, Tokyo, JP, V55/7, 1991, pp. 1817-1822.
Davis, Rowland,Neurospora, Contributions of a Model Organism, Oxford University Press, 2000. Book Not Sent.
Ellouz, S. et al., “Analaytical Separation ofTrichoderma reesei, Cellulases by Ion-Exchange Fast Protein Liquid Chromatography,” Journal of Chromatography, vol. 396, pp. 307-327, 1987.
Finkelstein, David B. et al., ed.,Biotechnology of Filamentous Fungi, Technology and Products, Chapter 6, pp. 113-156, Butterworth-Heinemann, Boston, MA, 1992.
Fliess, A. et al., “Characterization of Cellulases by HPLC Separation,” Eur. J. Appl. Microbiol. Biotechnol., vol. 17, pp. 314-318, 1983.
Flor, Perfecto Q. et al., “Production and Characteristics of Raw Starch-Digesting Glucoamylase O from a Protease-Negative, Glycosidase-NegativeAspergillus awamorivar.kawachiMutant,” Applied and Environmental Microbiology, vol. 34, No. 3, pp. 905-912, Mar. 1983.
Fujii, Michihiro et al., “Synergism of α-Amylase and Glucoamylase on Hydrolysis of Native Starch Granules,” Biotechnology and Bioengineering, vol. 32, pp. 910-915, 1988.
Goedegebuur, Frits et al., “Cloning and relational analysis of 15 novel fungal endoglucanases from family 12 glycosyl hydrolase,” Current Genetics, vol. 41, pp. 89-98, 2002.
Goto, Masatoshi et al., “The Mechanism of Binding of Glucoamylase I fromAspergillus awamorivar.kawachito Cyclodextrins and Raw Starch,” Biosci. Biotech. Biochem., vol. 58, No. 1, pp. 49-54, 1994.
Goyal, Anil et al., “Characteristics of Fungal Cellulases,” Bioresource Technology, vol. 36, pp. 37-50, 1991.
Hale & Markham, The Harper Collins Dictionary of Biology, Harper Perennial, NY, 1991.Book Not Sent.
Han, I et al.,“Amylolysis of Raw Corn byAspergillus nigerfor Simultaneous Ethanol Fermentation,”Biotechnology and Bioengineering, 30:225-233 (1987).
Harkki, A. et al., “A Novel Fungal Expression System : Secretion of Active Calf Chymosin from the Filamentous FungusTrichoderma Reesei,” Bio/Technology, vol. 7, pp. 596-603, Jun. 1989.
Harkki, Anu et al., “Genetic engineering ofTrichodermato produce strains with novel cellulase profiles,” Enzyme Microb. Technol., vol. 13, pp. 227-233, Mar. 1991.
Hata, Yoji et al., “The Glucoamylase cDNA fromAspergillus oryzae:Its Cloning, Nucleotide S
Dunn-Coleman Nigel
Lantz Suzanne E.
Pepsin Michael J.
Genencor International Inc.
Marcus-Wyner Lynn
Saidha Tekchand
LandOfFree
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