Cellulase preparation comprising an endoglucanase enzyme

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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Details

C435S006120, C435S320100, C435S252300, C435S254110, C435S325000, C536S023200, C536S024300, C536S024330

Reexamination Certificate

active

06423524

ABSTRACT:

FIELD OF INVENTION
The present invention concerns a cellulase preparation comprising a single-component endoglucanase, a detergent additive comprising the cellulase preparation, a detergent composition containing the cellulase preparation as well as methods of treating cellulose-containing fabrics with the cellulase preparation.
BACKGROUND OF THE INVENTION
It is well known in the art that repeated washing of cotton-containing fabrics generally causes a pronounced, unpleasant harshness in the fabric, and several methods for overcoming this problem have previously been suggested in the art. For example GB 1,368,599 of Unilever Ltd. teaches the use of cellulytic enzymes for reducing the harshness of cotton-containing fabrics. Also, U.S. Pat. No. 4,435,307 (of Novo Industri A/S) teaches the use of a cellulytic enzyme derived from
Humicola insolens
as well as a fraction thereof, designated AC
x
I, as a harshness reducing detergent additive. Other uses of cellulytic enzymes mentioned in the art involve soil removal from and colour clarification of fabric (cf. for instance EP 220 016), providing increasing water absorption (JP-B-52-48236) and providing a localized variation in colour to give the treated fabrics a “stone-washed” appearance (EP 307,564). Cellulytic enzymes may furthermore be used in the brewing industry for the degradation of &bgr;-glucans, in the baking industry for improving the properties of flour, in paper pulp processing for removing the non-crystalline parts of cellulose, thus increasing the proportion of crystalline cellulose in the pulp, and for improving the drainage properties of pulp, and in animal feed for improving the digestibility of glucans.
The practical exploitation of cellulytic enzymes has, to some extent, been set back by the nature of the known cellulase preparations which are often complex mixtures. It is difficult to optimise the production of multiple enzyme systems and thus to implement industrial cost-effective production of cellulytic enzymes, and their actual use has been hampered by difficulties arising from the need to apply rather large quantities of the cellulytic enzymes to achieve the desired effect on cellulosic fabrics.
The drawbacks of previously suggested cellulase preparations may be remedied by using preparations comprising a higher amount of endoglucanases. A cellulase preparation enriched in endoglucanase activity is disclosed in WO 89/00069.
SUMMARY OF THE INVENTION
A single endoglucanase component has now been isolated which exhibits favourable activity levels relative to cellulose-containing materials.
Accordingly, the present invention relates to a cellulase preparation consisting essentially of a homogeneous endoglucanase component which is immunoreactive with an antibody raised against a highly purified
~
43 kD endoglucanase derived from
Humicola insolens,
DSM 1800, or which is homologous to said
~
43 kD endoglucanase.
The finding that this particular endoglucanase component of cellulase is advantageous for the treatment of cellulose-containing materials is of considerable practical significance: it permits a cost-effective production of the cellulase, e.g. by employing recombinant DNA techniques for producing the active component, and makes the actual effective application of the enzyme feasible in that a smaller quantity of the cellulase preparation is requested to produce the desired effect on cellulosic materials.


REFERENCES:
patent: 4435307 (1984-03-01), Barbesgaard et al.
patent: WO 89/09259 (1989-10-01), None
Janson, J.C. (1984) Large-Scale Affinity Purification—State of the Art and Future Prospects. Trends in Biotechnol. 2(2): 31-38.*
Wood et al. Methods in Enzymology 160:323-32 (1988).
Poulsen et al. Chem. Abs. 107(9):292 No. 73161r (1987).
Klesov et al. Chem. Abs.106(17):302 No. 134159z (1987).
Ortega, Chem. Abs.114(15):619 No. 141530g (1991).
Rao et al. Chem. Abs. 105(13):307 No. 110894p (1986).
Hayashida et al. Chem. Abs. 105(3):316 No. 20820g (1986).

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