Trichoderma reesei glucoamylase and homologs thereof

Details Trichoderma reesei glucoamylase and homologs thereof Trichoderma reesei glucoamylase and homologs thereof

2011-04-05

2011-04-05

Raghu, Ganapathirama (Department: 1652)

Chemistry: molecular biology and microbiology

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

Hydrolase

C435S203000, C435S200000, C435S262000, C435S161000, C435S096000, C435S099000, C435S022000, C510S305000, C510S320000, C510S392000, C536S023200, C536S023700

Reexamination Certificate

active

07919299

ABSTRACT:
The present invention is related to glucoamylases having at least 80% sequence identity to a Trichoderma glucoamylase having the sequence of SEQ ID NO: 4 and biologically functional fragments thereof. The invention is also related to DNA sequences coding for the glucoamylases, vectors and host cells incorporating the DNA sequences, enzyme compositions and methods of using the glucoamylases in various applications.

REFERENCES:
patent: 4247637 (1981-01-01), Tamura et al.
patent: 4514496 (1985-04-01), Yoshizumi et al.
patent: 4618579 (1986-10-01), Dwiggins et al.
patent: 4794175 (1988-12-01), Numberg et al.
patent: 4863864 (1989-09-01), Ashikari et al.
patent: 5024941 (1991-06-01), Maine et al.
patent: 5246853 (1993-09-01), Clarkson et al.
patent: 5475101 (1995-12-01), Ward et al.
patent: 5665585 (1997-09-01), Torkkeli et al.
patent: 5847276 (1998-12-01), Mimken et al.
patent: 6022725 (2000-02-01), Fowler et al.
patent: 6254914 (2001-07-01), Singh et al.
patent: 6255084 (2001-07-01), Nielsen et al.
patent: 6268328 (2001-07-01), Mitchinson et al.
patent: 6309872 (2001-10-01), Rey et al.
patent: 6620924 (2003-09-01), Nielsen et al.
patent: 6899910 (2005-05-01), Johnston et al.
patent: 7413879 (2008-08-01), Dunn-Coleman et al.
patent: 7494685 (2009-02-01), Dunn-Coleman et al.
patent: 0 244 234 (1993-07-01), None
patent: 0 238 023 (1993-12-01), None
patent: 0 215 594 (1995-11-01), None
patent: WO 88/09795 (1988-12-01), None
patent: WO 92/06209 (1992-04-01), None
patent: WO 96/00787 (1996-01-01), None
patent: WO 02/46429 (2002-06-01), None
patent: WO 03/068976 (2003-08-01), None
patent: WO 2004/080923 (2004-09-01), None
patent: WO 2004/081193 (2004-09-01), None
patent: WO 2005/001036 (2005-01-01), None
patent: WO 2005/052148 (2005-06-01), None
Broun et al., Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. Science, 1998, vol. 282: 1315-1317.
Devos et al., Practical limits of function prediction. Proteins: Structure, Function, and Genetics. 2000, vol. 41: 98-107.
Aleshin, A et al. “Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-A resolution.”Journal of Biological Chemistry267(27):19291-19298, 1992.
Alexopoulos, C.J. et al. “Phylum Ascomycota.” InIntroductory Mycology, New York: John Wiley & Sons, pp. 323-375, 1996.
Altschul, S.F. et al. “Basic local alignment search tool.”J. Mol. Biol215(3):403-410, 1990.
Ashikari, T. et al. “Direct fermentation of raw corn to ethanol by yeast transformants containing a modified Rhizopus glucoamylase gene.”Applied Microbiology and Biotechnology32(2):129-133, 1989.
Ashikari, T. et al. “Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast.”Agricultural and biological chemistry50(4):957-964, 1986.
Barnett et al., “Cloning and amplification of the gene encoding an extracellular beta-glucosidase fromTrichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates,”Bio/Technology, V.9:Jun. 9, 1991, pp. 562-567.
Boel, E., M T Hansen, et al. “Two different types of intervening sequences in the glucoamylase gene from Aspergillus niger.”EMBO J. 3(7):1581-1585, 1984.
Boel, E., I. Hjort, et al. “Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs.”The EMBO Journal3(5):1097-1102, 1984.
Brosius, J. “Superpolylinkers in cloning and expression vectors.”DNA(Mary Ann Liebert, Inc.) 8(10):759-777, 1989.
Brown, T. A. “How to obtain a clone of a specific gene.” InGene Cloning: An Introduction, London: Chapman and Hall, pp. 159-182, 1995.
Campbell, E.I. et al. “Improved transformation efficiency of Aspergillus niger using the homologous niaD gene for nitrate reductase.”Current Genetics16(1):53-56, 1989.
Chambergo et al., “Elucidation of the metabolic fate of glucose in the filamentous fungusTrichoderma reeseiusing espressed sequence tag (EST) analysis and cDNA microarrays,”J. of Biological Chemistry, Apr. 19, 2002, V. 277 :16, pp. 13983-13988.
Cao, Q.N. et al. “Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).”Protein Sci9(5):991-1001, 2000.
Database EMBL Nov. 20, 2003, “TrEST-A0518 TrEST-A Hypocrea jecorina cDNA clone Tr-A0518 5′ similar to glucan 1,4-alpha-glucosidase (EC 3.2.1.3) precuror—Neurospora crassa, m RNA sequence.” Retrieved from EBI accession No. EM—PRO:CF944444.
Database EMBL Nov. 20, 2003, “TrEST-A0916 TrEST-A Hypocrea jecorina cDNA clone Tr-A0916 5′ similar to glucan 1,4-alpha-glucosidase (EC 3.2.1.3) precursor—Neurospora crassa, mRNA sequence.” Retrieved from EBI accession No. EM—PRO:CF943925.
Database EMBL Nov. 20, 2003, “TrEST-A2623 Trest-A Hypocrea jecorina CDNA clone Tr-A2623 5′ similar to glucan1,4-alpha-glucosidase (EC 3.2.1.3) precuror—Neurospora crassa, MRNA sequence.” Retrieved from EBI accession No. EM—PRO:CF944284.
Database EMBL Apr. 26, 2003 “tric021xg09T.reeseimycelial culture, Version 3 April Hypocrea jecorina cDNA clone tric021xg09, mRNA sequence.”retrived from EBI accession No. EM—PRO:CB900226.
Database EMBL Feb. 6, 2002, “TrEST-A4050 TrEST-A Hypocrea jecorina cDNAclone Tr-A4050 5′ similar to glucoamylase, mRNA sequence.” Retrieved from EBI accession No. EM—PRO:BM076396.
Database Genbank. “Trichoderma reeseicbh1 gene for cellobiohydrolase I, upstream region.” Accession No. D86235, 1997.
Dayhoff, M.O. et al. “A Model of Evolutionary Change in Proteins.” InAtlas of Protein Sequence and Structure, ed. M.O. Dayhoff. Silver Spring, MD: National Biomedical Research Foundation, pp. 345-352, 1978.
Edman, P. “Synthesis of 3-phenyl-2-thiohydantoin.”Acta Chem. Scand. 10:761-8, 1956.
Elder, M.T. et al. “Glucoamylase activity in industrial enzyme preparations using colorimetric enzymatic method: collaborative study.”Journal of AOAC International78(2):398-401, 1995.
Fagerstrom et al., “Characterization, subsite mapping and partial bamino acid sequence of glucoamylase from the filamentous fungusTrichoderma reesei.”Biotechnology and Applied Biochemistry Res. Lab., Alko Ltd., V.21 :2, 1995, pp. 223-231.
Fagerstrom et al., “Purification and specificity of recombinant Hormoconis resinae glucoamylase P and endogenous glucoamylase fromTrichoderma reesei,” Enzyme and Microbial Technology, V.16 :1, 1994, pp. 36-42.
Finkelstein, D.B. “Transformation.” InBiotechnology of Filamentous Fungi: Technology and Products, eds. D.B. Finkelstein et al. Boston, MA: Butterworth-Heinemann, pp. 113-156, 1992.
Goto, M. et al. “The Mechanism of Binding of Glucoamylase I from Aspergillus awamori var. kawachi to Cyclodextrins and Raw Starch.”Bioscience, biotechnology, and biochemistry58(1):49-54, 1994.
de Groot, M.J.A. et al. “Agrobacterium tumefaciens-mediated transformation of filamentous fungi.”Nat Biotech16(9):839-842, 1998.
Guo, H.H. et al. “Protein tolerance to random amino acid change.”Proc. Natl. Acad. Sci. U.S.A101(25):9205-10, 2004.
Harkki, A. et al. “Genetic engineering of Trichoderma to produce strains with novel cellulase profiles.”Enzyme Microb. Technol13(3):227-33, 1991.
Harkki A. et al. “A Novel Fungal Expression System: Secretion of Active Calf Chymosin from the Filamentous FungusTrichoderma reesei.” Bio/Technology7(6):596-603, 1989.
Hartley, J.L. et al. “DNA cloning using in vitro site-specific recombination.”Genome Research10(11):1788-1795, 2000.
Hayashida, S. et al. “Molecular cloning of the glucoamylase I gene of Aspergillus awamori var. kawachi for localization of the raw-starch-affinity site.”Agricultural and Biological Chemistry53(4):923-929, 1989.
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