Cellulases and their uses

Details Cellulases and their uses Cellulases and their uses

2005-04-29

2010-06-22

Raghu, Ganapathirama (Department: 1652)

Chemistry: molecular biology and microbiology

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

Hydrolase

C435S183000, C435S262000, C435S263000, C510S114000, C510S300000, C510S305000, C510S374000, C510S392000, C510S531000, C510S535000, C536S023200, C536S023400, C536S023700

Reexamination Certificate

active

07741093

ABSTRACT:
The present invention provides novel cellulase fusion proteins, preparations of cellulase fusion proteins and compositions of cellulase fusion proteins. The present invention further provides cellulase expression vectors, host cells expressing cellulase and methods for preparing such vectors and cells. Uses of cellulases, cellulase preparations and cellulase compositions in the textile, detergent, pulp and paper industries are also provided.

REFERENCES:
patent: 3664961 (1972-05-01), Norris
patent: 5433750 (1995-07-01), Gradinger et al.
patent: 5443750 (1995-08-01), Convents et al.
patent: 5770418 (1998-06-01), Yaver et al.
patent: 5792641 (1998-08-01), Schuelein et al.
patent: 5837515 (1998-11-01), Suominen et al.
patent: 5843745 (1998-12-01), Berka et al.
patent: 5989899 (1999-11-01), Bower et al.
patent: 6184019 (2001-02-01), Miettinen-Oinonen et al.
patent: 0 238 216 (1987-09-01), None
patent: 0 244 234 (1987-11-01), None
patent: 0 663 950 (1995-07-01), None
patent: WO 91/17244 (1991-11-01), None
patent: WO 94/07998 (1994-04-01), None
patent: WO 95/33386 (1995-12-01), None
patent: WO 96/29397 (1996-09-01), None
patent: WO 97/08325 (1997-03-01), None
patent: 9714804 (1997-04-01), None
patent: WO 97/14804 (1997-04-01), None
patent: WO 98/12307 (1998-03-01), None
patent: WO 2004/016760 (2004-02-01), None
Broun et al., Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. Science, 1998, vol. 282: 1315-1317.
Witkowski et al., Conversion of b-ketoacyl synthase to a malonyl decarboxylase by replacemnt of the active-site cysteine with glutamine. Biochemistry, 1999, vol. 38: 11643-11650.
Seffernick et al., Melamine deaminase and Atrazine chlorohydrolase: 98 percent identical but functionally different. J. Bacteriol.,2001, vol. 183 (8): 2405-2410.
Guo et al., Protein tolerance to random amino acid change. PNAS., 2004, vol. 101 (25): 9205-9210.
Joutsjoki et al., “Transformation ofTrichoderma reeseiwith theHormoconis resinaeglucoamylase P (gamP) gene: production of a heterologous glucoamylase byTrichoderma reesei.,” Curr. Genet., 24:223-228 (1993).
Kim et al., “Functional Analysis of a Hybrid Endoglucanase of Bacterial Origin Having a Cellulose Binding Domain from a Fungal Exoglucanase,”Applied Biochem. Biotech., 75:193-204 (1998).
Srisodsuk et al., “Trichoderma reeseicellobiohydrolase I with an endoglucanase cellulose-binding domain: action on bacterial microcrystalline cellulose,”J. Biotech.,57:49-57 (1997).
Hong et al., “Cloning of a gene encoding thermostable cellobiohydrolase fromThermoascus aurantiacusand its expression in yeast,”Appl. Microbiol. Biotechnol., 63:42-50 (2003).
Karhunen et al., “High frequency one-step gene replacement inTrichoderma reesei. I. Endoglucanase I overproduction,”Mol. Gen. Genet., 241:515-522 (1993).
Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,”Nature, 227:680-685 (1970).
Linder et al., “Identification of functionally important amino acids in the cellulose-binding domain ofTrichoderma reeseicellobiohydrolase I,”Protein Science, 4:1056-1064 (1995).
Lowry et al., “Protein measurement with the Folin phenol reagent,”J. Biol. Chem., 193:265-275 (1951).
Malardier et al., “Cloning of the nitrate reductase gene (niaD) ofAspergillus nidulansand its use for transformation ofFusarium oxysporum,”Gene, 15:147-156 (1989).
Miettinen-Oinonen et al., “Three cellulases fromMelanoarpus albomyceswith applications in the textile industry,”Enz. Microbiol. Technol. 34:332-341 (2004).
Penttilä et al., “A versatile transformation system for the cellulolytic filamentous fungusTrichoderma reesei,” Gene, 61:155-164 (1987).
Saloheimo et al., “A novel, small endoglucanase gene,egl5, fromTrichoderma reeseiisolated by expression in yeast,”Mol. Microbiol., 13:219-228 (1994).
Srisodsuk et al., “Role of the interdomain linker peptide ofTrichoderma reeseicellobiohydrolase I in its interaction with crystalline cellulose,”J. Biol. Chem., 268:20756-20761 (1993).
Aho et al., “Monoclonal antibodies against core and cellulose-binding domains ofTrichoderma reeseicellobiohydrolases I and II and endoglucanase I,”Eur. J. Biochem., 200:643-649 (1991).
Azevedo et al., “Cloning, sequencing and homologies of the cbh-1 (exoglucanase) gene ofHumicola griseavar.thermoidea,” J. Gen. Microbiol., 136: 2569-2576, (1990).
Bailey and Nevalainen, “Induction, isolation and testing of stableTrichoderma reeseimutants with improved production of solubilizing cellulose,”Enz. Microbiol. Technol., 3: 153-157 (1981).
Haakana et al., “Cloning of cellulase genes fromMelanocarpus albomycesand their efficient expression inTrichoderma reesei,” Enz. Microbiol. Technol., 34: 159-167 (2004).
Henrissat, “A classification of glycosyl hydrolases based on amino acid sequence similarities,”Biochem. J., 280: 309-316 (1991).
Henrissat and Bairoch, “New families in the classification of glycosyl hydrolases based on amino acid sequence similarities,”Biochem. J., 293:781-788 (1993).
van Tilbeurgh et al., “Fluorogenic and chromogenic glycosides as substrates and ligands of carbohydrases,”Meth. Enzymol., 160:45-59 (1988).
Ward et al., “Cloning, sequence and preliminary structural analysis of a small, high pI endoglucanase (EGIII) fromTrichoderma reesei,” Proceedings of the second TRICEL symposium on Trichoderma Reesei Cellulases and Other Hydrolases, Espoo, Finland, ed. by P. Suominen and T. Reinikainen; Foundation for Biotechnical and Industrial Fermentation Research; 8:153-158 (1993).
English abstract of WO 95/33386.
AC# AF478686, Oct. 31, 2003.
AC# AJ515703, May 12, 2005.
AC# AJ515704, May 12, 2005.
AC# AJ515705, May 12, 2005.
AC# AR088330, Sep. 7, 2000.
Supplementary European Search Report for corresponding EP 06 72 5936, Jun. 9, 2009.
Gustavsson, Malin, et al., “Stable linker peptides for a cellulose-binding domain-lipase fusion protein expressed inPichia pastoris,” Protein Engineering, May 31, 2001 (revised), pp. 711-715, vol. 14 No. 9, Oxford University Press. (XP009118009).

Affiliated with

Also associated with

Rating

Cellulases and their uses does not yet have a rating. At this time, there are no reviews or comments for this patent.

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

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4233223