Endoglucanases

Details Endoglucanases Endoglucanases

1999-01-13

2002-05-14

Slobodyansky, Elizabeth (Department: 1652)

Chemistry: molecular biology and microbiology

Process of utilizing an enzyme or micro-organism to destroy...

Textile treating

C435S209000, C435S277000, C570S185000, C570S185000

Reexamination Certificate

active

06387690

ABSTRACT:

FIELD OF THE INVENTION
The present invention relates to novel enzyme preparations comprising an enzyme exhibiting endoglucanase activity which performs very good in industrial applications such as laundry compositions, for biopolishing of newly manufactured textiles, for providing an abraded look of cellulosic fabric or garment, and for treatment of paper pulp. Further, the invention relates to DNA constructs encoding such enzymes, a method for providing a gene encoding for such enzymes, a method of producing the enzymes, enzyme preparations containing such enzymes, and the use of these enzymes for a number of industrial applications.
BACKGROUND OF THE INVENTION
Cellulases or cellulloytic enzymes are enzymes involved in hydrolyses of cellulose. In the hydrolysis of native cellulose, it is known that there are three major types of cellulase enzymes involved, namely cellobiohydrolase (1,4-&bgr;-D-glucan cellobiohydrolase, EC 3.2.1.91), endo-&bgr;-1,4-glucanase (endo-1,4-&bgr;-D-glucan 4-glucanohydrolase, EC 3.2.1.4) and &bgr;-glucosidase (EC 3.2.1.21).
Cellulases are synthesized by a large number of microorganisms which include fungi, actinomycetes, myxobacteria and true bacteria but also by plants. Especially endoglucanases of a wide variety of specificities have been identified.
A very important industrial use of cellulytic enzymes is the use for treatment of cellulosic textile or fabric, e.g. as ingredients in detergent compositions or fabric softener compositions, for bio-polishing of new fabric (garment finishing), and for obtaining a “stone-washed” look of cellulose-containing fabric, especially denim, and several methods for such treatment have been suggested, e.g. in GB-A-1 368 599, EP-A-0 307 564 and EP-A-0 435 876, WO 91/17243, WO 91/10732, WO 91/17244, PCT/DK95/000108 and PCT/DK95/00132.
Another important industrial use of cellulytic enzymes is the use for treatment of paper pulp, e.g. for improving the drainage or for deinking of recycled paper.
Especially the endoglucanases (EC No. 3.2.1.4) constitute an interesting group of hydrolases for the mentioned industrial uses. Endoglucanases catalyses endo hydrolysis of 1,4-&bgr;-D-glycosidic linkages in cellulose, cellulose derivatives (such as carboxy methyl cellulose and hydroxy ethyl cellulose), lichenin, &bgr;-1,4 bonds in mixed &bgr;-1,3 glucans such as cereal &bgr;-D-glucans or xyloglucans and other plant material containing cellulosic parts. The authorized name is endo-1,4-&bgr;-D-glucan 4-glucano hydrolase, but the abbreviated term endoglucanase is used in the present specification. Reference can be made to T.-M. Enveri, “Microbial Cellulases” in W. M. Fogarty, Microbial Enzymes and Biotechnology, Applied Science Publishers, p. 183-224 (1983); Methods in Enzymology, (1988) Vol. 160, p. 200-391 (edited by Wood, W. A. and Kellogg, S. T.); Béguin, P., “Molecular Biology of Cellulose Degradation”, Annu. Rev. Microbiol. (1990), Vol. 44, pp. 219-248; Béguin, P. and Aubert, J-P., “The biological degradation of cellulose”, FEMS Microbiology Reviews 13 (1994) p.25-58; Henrissat, B., “Cellulases and their interaction with cellulose”, Cellulose (1994), Vol. 1, pp. 169-196.
Fungal endoglucanases have been described in numerous publications, especially those derived from species as e.g.
Fusarium oxysporum, Trichoderma reesei, Trichoderma longibrachiatum, Aspergillus aculeatus, Neocallimastix patriciarum
, and e.g. from species of the genera Piromyces, Humicola, Myceliophthora, Geotricum, Penicillium, Irpex, Coprinus.
For example, fungal endoglucanases have been described by Sheppard, P. O., et al., “The use of conserved cellulase family-specific sequences to clone Cellulase homologue cDNAs from
Fusarium oxysporum
, Gene, (1994), Vol. 15, pp. 163-167, Saloheimo, A., et al., “A novel, small endoglucanase gene, egI5, from
Trichoderma reesei
isolated by expression in yeast”, Molecular Microbiology (1994), Vol. 13(2), pp. 219-228; van Arsdell, J. N. et al., (1987), Cloning, characterization, and expression in
Saccharomyces cerevisiae
of endoglucanase I from
Trichoderma reesei
, Bio/Technology 5: 60-64; Penttilä, M. et al., (1986), “Homology between cellulase genes of
Trichoderma reesei
: complete nucleotide sequence of the endoglucanase I gene”,
Gene
45:253-263; Saloheimo, M. et al, (1988), “EGIII, a new endoglucanase from
Trichoderma reesei
: the characterization of both gene and enzyme”,
Gene
63:11-21; Gonzáles, R., et al., “Cloning, sequence analysis and yeast expression of the egl1 gene from
Trichoderma longibrachiatum
”, Appl. Microbiol. Biotechnol., (1992), Vol. 38, pp. 370-375; Ooi, T. et al. “Cloning and sequence analysis of a cDNA for cellulase (FI-CMCase) from
Aspergillus aculeatus
”, Curr. Genet., (1990), Vol. 18, pp. 217-222; Ooi, T. et al, “Complete nucleotide sequence of a gene coding for
Aspergillus aculeatus
cellulase (FI-CMCase)”, Nucleic Acids Research, (1990), Vol. 18, No. 19, p. 5884; Xue, G. et al., “Cloning and expression of multiple cellulase cDNAs from the anaerobic rumen fungus
Neocallimastix patriciarum
in
E. coli
”, J. Gen. Microbiol., (1992), Vol. 138, pp. 1413-1420; Xue, G. et al., “A novel polysaccharide hydrolase cDNA (celD) from
Neocallimastix patriciarum
encoding three multi-functional catalytical domains with high endoglucanase, cellobiohydrolase and xylanase activities”, J. Gen. Microbiol., (1992), Vol. 138, pp. 2397-2403; Zhou, L. et al., “Intronless celB from the anaerobic fungus
Neocallimastix patriciarum
encodes a modular family A endoglucanase”, Biochem. J., (1994), Vol. 297, pp. 359-364; Dalbøge, H. and Heldt-Hansen, H. P., “A novel method for efficient expression cloning of fungal enzyme genes”, Mol. Gen. Genet., (1994), Vol. 243, pp. 253-260; Ali, B. R. S. et al., “Cellulases and hemicellulases of the anaerobic fungus
Piromyces constitute
a multiprotein cellulose-binding complex and are encoded by multigene families”, FEMS Microbiol. Lett., (1995), Vol. 125, No. 1, pp. 15-21. Further, the DNA Data Bank of Japan (DDBJ database publicly available at Internet) comprises two DNA sequences cloned from
Penicillium janthinellum
encoding endoglucanases (cloned by A. Koch and G. Mernitz, respectively) and a DNA sequence cloned from
Humicola grisea
var. thermoidea encoding an endoglucanase (cloned by T. Uozumi). Two endoglucanases from
Macrophomina phaseolina
have been cloned and sequenced, see Wang, H. Y. and Jones, R. W.: “Cloning, characterization and functional expression of an endoglucanase-encoding gene from the phytopathogenic fungus
Macrophomina phaseolina
” in Gene, 158:125-128, 1995, and Wang, H. Y. and Jones, R. W.: “A unique endoglucanase-encoding gene cloned from the phytopathogenic fungus
Macrophomina phaseolina
” in Applied And Environmental Microbiology, 61:2004-2006, 1995. One of these endoglucanases shows high homology to the egl3 endoglucanase from the fungus
Trichoderma reesei
, the other shows homology to the egl1 from the microbial phytopathogen
Pseudomonas solanacearum
indicating that both endoglucanases belong to family 5 of glycosyl hydrolases (B. Henrissat, Biochem J 280:309-316 (1991)). Filament-specific expression of a cellulase gene in the dimorphic fungus
Ustilago maydis
is disclosed in Schauwecker, F. et al. (1995).
WO 91/17243 (Novo Nordisk A/S) discloses a cellulase preparation consisting of a homogenous endoglucanase component immunoreactive with an antibody raised against a highly purified 43 kDa endoglucanase derived from
Humicola insolens
, DSM 1800; WO 91/17244 (Novo Nordisk A/S) discloses a new (hemi)cellulose degrading enzyme, such as an endoglucanase, a cellobiohydrolase or a &bgr;-glucosidase, which may be derived from fungi other than Trichoderma and Phanerochaete; WO 93/20193 discloses an endoglucanase derivable from
Aspergillus aculeatus
; WO 94/21801 (Genencor Inc.) concerns a cellulase system isolated from
Trichoderma longibrachiatum
exhibiting endoglucanase activity; WO 94/26880 (Gist Brocades N.V.) discloses an isolated mixture of cellulose degrading enzymes, which preferable are obtained from Trichoderma, A

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