BGL3 beta-glucosidase and nucleic acids encoding the same

Details BGL3 beta-glucosidase and nucleic acids encoding the same BGL3 beta-glucosidase and nucleic acids encoding the same

2011-06-14

2011-06-14

Fronda, Christian L (Department: 1652)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Preparing compound containing saccharide radical

C435S183000, C435S200000, C435S252300, C435S320100, C536S023200

Reexamination Certificate

active

07960146

ABSTRACT:
The present invention provides a novel β-glucosidase nucleic acid sequence, designated bgl3, and the corresponding BGL3 amino acid sequence. The invention also provides expression vectors and host cells comprising a nucleic acid sequence encoding BGL3, recombinant BGL3 proteins and methods for producing the same.

REFERENCES:
patent: 4435307 (1984-03-01), Barbesgaard et al.
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 4822516 (1989-04-01), Suzuki et al.
patent: 5475101 (1995-12-01), Ward et al.
patent: 5648263 (1997-07-01), Schulein et al.
patent: 5691178 (1997-11-01), Schulein et al.
patent: 5776757 (1998-07-01), Schulein et al.
patent: 6004785 (1999-12-01), Berka et al.
patent: 6022725 (2000-02-01), Fowler et al.
patent: 6162782 (2000-12-01), Clarkson et al.
patent: 6184018 (2001-02-01), Li et al.
patent: 0 562 003 (2002-09-01), None
patent: 1368599 (1974-10-01), None
patent: 2 094 826 (1982-09-01), None
patent: 2 095 275 (1982-09-01), None
patent: WO 91/04673 (1991-04-01), None
Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84.
Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23.
Altschul, Stephen F. et al., “Basic Local Alignment Search Tool,” J. Mol. Biol. 215:403-410, 1990.
Altschul, Stephen F. et al., “Gapped BLAST and PSI-BLAST: a new generation of protein database search programs,” Nucl. Acids Res., vol. 25, pp. 3389-3402, 1997.
Aro, Nina et al., “ACEII, a Novel Transcriptional Activator Involved in Regulation of Cellulase and Xylanase Genes ofTrichoderma reesei,” J. Biol. Chem., vol. 276, No. 26, pp. 24309-24314, Jun. 29, 2001.
Aubert, et al., Ed., p11 et seq., Academic Press, 1988.
Ausubel, G. M. et al. Current Protocols in Molecular Biology, John Wiley & Sons, New York, NY, 1993.
Baldwin, Don et al., Curr. Opin. Plant Biol. 2(2):96-103, 1999.
Barnett, Christopher et al. “Cloning and Amplification of the Gene Encoding an Extracellular β-Glucosidase fromTrichoderma reesei: Evidence for Improved Rates of Saccharification of Cellulosic Substrates,” Bio/Technology, 9:562-567 (1991).
Baulcombe, D., “ Viruses and gene silencing in plants,” 100 Years of Virology, Calisher and Horzinek eds., Springer-Verlag, New York, NY 15:189-201, 1999.
Bhikhabhai, R. et al., “Isolation of Cellulolytic Enzymes fromTrichoderma reeseiQM 9414,” J. Appl. Biochem. 6:336-345, 1984.
Brumbauer, Aniko et al., Fractionation of cellulase and β-glucosidase in aTrichoderma reeseiculture liquid by use of two-phase partitioning, Bioseparation 7:287-295, 1999.
Carter, Paul et al., “Improved oligonucleotide site-directed mutagenesis using M13 vectors,”Nucleic Acids Research, vol. 13, No. 12, pp. 4431-4443, 1985.
Cees, Am. M. et al., “Heterologous Gene Expression in Filamentous Fungi,” More Gene Manipulations in Fungi, Bennett and Lasure, ed., pp. 397-428, 1991.
Chen, Huizhong et al., “Purification and characterization of two extracellular β-glucosidases fromTrichoderma reesei” Biochem et Biophysica Acta 1121:54-60 (1992).
Coligan, J. E. et al., eds., Current Protocols in Immunology, 1991.
Collen, Anna et al., Journal of Chromatography A 910:275-284, 2001.
Coughlan, Michael et al., “Comparative Biochemistry of Fungal and Bacterial Cellulolytic Enzyme Systems” Biochemistry and Genetics of Cellulose Degradation, pp. 11-30 1988.
Cummings, C. et al., “Secretion ofTrichoderma reeseiβ-glucosidase bySaccharomyces cerevisiae,” Curr. Genet. 29:227-233, 1996.
Dayhoff, M.O. et al., “A Model of Evolutionary Change in Proteins,” Atlas of Protein Sequence and Structure, National Biomedical Research Foundation, Washington, D.C., vol. 5, Supplement 3, Chapter 22, pp. 345-352 1978.
Deutscher, Murray P., “Rethinking Your Purification Procedure,” Methods in Enzymology, vol. 182, No. 57, pp. 779, 1990.
Doolittle, R. F., Of URFs and ORFs, University Science Books, CA, 1986.
Ellouz, S. et al., “Analytical Separation ofTrichoderma reeseiCellulases by Ion-Exchange Fast Protein Liquid Chromatography,” J. Chromatography 396:307-317, 1987.
Fields, Stanley et al., “A novel genetic system to detect protein-protein interactions,” Nature, 340:245-246, 1989.
Filho, Edivaldo, “Purification and characterization of a β-glucosidase from solid-state cultures ofHumicola griseavar.thermoidea,” Can. J. Microbiol. 42:1-5, 1996.
Fliess, A. et al., “Characterization of Cellulases by HPLC Separation,” Eur. J. Appl. Microbiol. Biotechnol. 17:314-318, 1983.
Freer, Shelby, “Kinetic Characterization of a β-Glucosidase from a Yeast,Candida wickerhamii,” J. Biol. Chem. vol. 268, No. 13, pp. 9337-9342, 1993.
Freshney, R. I., ed., Animal Cell Culture, 1987.
Goyal, Anil et al. “Characteristics oif Funal Cellulases,” Bioresource Technol. 36:37-50, 1991.
Halldorsdottir, S et al., “Cloning, sequencing and overexpression of aRhodothermus marinusgene encoding a thermostable cellulase of glycosyl hydrolase family 12,” Appl Microbiol Biotechnol. 49(3):277-84, 1998.
Hemmpel, W.H., “The surface modificaitonof woven and knitted cellulose fibre fabrics by enzymatic degradation,” ITB Dyeing/Printing/Finishing 3:5-14, 1991.
Henrissat, Bernard et al., “New families in the classification of glycosyl hydrolases based on amino acid sequence similarities,” Biochem. L. 293:781-788, 1993.
Herr, D. et al., “Purification and Properties of an Extracellular β-Glucosidase fromLenzites trabea,” European Appl. Microbiol. Biotechnol. 5:29-36, 1978.
Hu, Qianjin et al., “Antibodies Specific for the Human Retinoblastoma Protein Identify a Family of Related Polypeptides,” Mol Cell Biol. vol. 11, No. 11, pp. 5792-5799, 1999.
Ilmen, Marja et al., “Regulation of Cellulase Gene Expression in the Filamentous FungusTrichoderma reesei,” Appl. and Envir. Micro., vol. 63, No. 4, pp. 1298-1306, 1997.
Iwashita, Kazuhiro et al. “ThebglAGene ofAspergillus kawachiiEncodes Both Extracellular and Cell Wall-Bound β-Glucosidases,” Appl. Env. Microbiology, vol. 65, No. 12, pp. 5546-5553, 1999.
Jakobovits, Aya, et al., “Production of Antigen-Specific Human Antibodies from Mice Engineered with Human Heavy and Light Chain YACs” Annals New York Academy of Sciences, 764:525-535, 1995.
Jakobovits, Aya, “Production of fully human antibodies by transgenic mice,” Curr Opin Biotechnol 6(5):561-6, 1995.
Jones, Peter et al., “Replacing the complementarity—determining region sin a human antibody with those from a mouse,” Nature 321:522-525, 1986.
Kawaguchi, Takashi et al., “Cloning and sequencing of the cDNA encoding β-glucosidase 1 fromAspergillus aculeatus,” Gene 173(2):287-8, 1996.
Knowles, Jonathan et al., TIBTECH 5, 255-261, 1987.
Kohler, G. et al., “Continuous cultures of fused cells secreting antibody of predefined specificity,” Nature, vol. 256, pp. 495-499, Aug. 7, 1975.
Krishna, S. Hari et al., “Simultaneous saccharification and fermentation of lignocellulosic wastes to ethanol using a thermotolerant yeast,” Bioresource Tech. 77:193-196, 2001.
Kumar, Akhil, et al., “Optimizing the Use of Cellulase Enzymes in Finishing Cellulosic Fabrics,” Textile Chemist and Colorist, 29:37-42, 1997.
Lehtio, Janne. et al., FEMS Microbiology Letters 195:197-204, 2001.
Li, Xin-Liang et al. “Expression ofAureobasidium pullulans xynAin, and Secretion of the Xylanase from,Saccharomyces cerevisiae,” Appl. Environ. Microbiol. 62, No. 1, pp. 209-213, 1996.
Linder, Marcus et al., “The roles and function of cellulose-binding domains,” Journal of Biotechnol. 57:15-28, 1997.
Liukkonen, Pere J., et al., “Use of Purified Enzymes in Mechanical Pulping,” 1996 Tappi Pulping Conference, pp. 693-696, Nashville, TN.
Loftus, Joseph C. et al. “A β3

Affiliated with

Also associated with

Rating

BGL3 beta-glucosidase and nucleic acids encoding the same does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with BGL3 beta-glucosidase and nucleic acids encoding the same, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and BGL3 beta-glucosidase and nucleic acids encoding the same will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2649629