Enzyme exhibiting mannanase activity

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

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4353201, 4352523, 43525411, 4352543, 536 232, C12N 924, C12N 1500, C12N 114, C07H 2104

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active

057957649

DESCRIPTION:

BRIEF SUMMARY
CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a continuation of PCT/DK94/00174 filed Apr. 28, 1994, which is incorporated herein by reference.


FIELD OF INVENTION

The present invention relates to an enzyme with mannanase activity, a method of producing the enzyme, and an enzyme preparation containing the enzyme.


BACKGROUND OF THE INVENTION

Mannanases (EC 3.2.1.78) consitute a group of polysaccharases which degrade mannans. Mannan containing polysaccharides are a major component of the the hemicellulose fraction in both hardwoods and softwoods as well as in the endosperm in many leguminous seeds and in some mature seeds of non-leguminous plants (Dekker 1979; Araujo and Ward 1990). Essentially unsubstituted linear .beta.-1,4-mannan is found in some non-leguminous plants (e.g. Phytelepas macrocarpa, or ivory nut). Unsubstituted .beta.-1,4-mannan resembles cellulose in the conformation of the individual polysaccharide chains, and it is water insoluble. In leguminous seeds, water soluble galactomannan is the main storage carbohydrate, comprising up to 20% of the total dry weight in some cases (McCleary 1988). Galctomannan has .alpha.-galactose linked to O-6 of mannose residues and it can also be acetylated to various degrees on O-2 and O-3 of the mannose residues.
Mannans are also known from several monocotyledonous plants, and is found to be the most abundant polysaccharide in the cell walls material in palm kernel meal (Dusterhoft et al.; J. Sci. Food Agric 55 (1991) 411-422). Glucomannans are linear polysaccharides with more or less regularly alternating .beta.-1,4 linked mannose and glucose. Glucomannans are found in e.g. konjac (Amorphophallus konjac).
Mannans, galactomannans, glucomannans and galactoglucomannans (glucomannans which galactose sidebranches) contributes more than 50% of the softwood hemicelluloses. Furthermore, the cellulose of many red algae contains a significant amount of mannose, e.g. the so-called .alpha.-cellulose from Porphyra is pure mannan.
Mannanases which are capable of cleaving glycosidic bonds in mannans, glucomannans, galactomannans and galactoglucomannans are useful enzymes within the food, oil, paper, and textile industry.
Mannases have been purified from a different sources (Dekker 1979). The majority of the .beta.-mannanases which have been purified to homogeneity and/or cloned have been isolated from either prokaryots or from plants (Araujo and Ward 1990; Gibbs, Saul et al. 1992; Arcand, Kluepfel et al. 1993; Henrissat 1993). Fungal mannanases have been described by McCleary (1988) (an Aspergillus niger mannanase), Araujo and Ward (1990), and Johnson (1990).
WO 93/24622 published only after the priority date of the present invention describes a mannanase isolated from Trichoderma reesei and the DNA sequence encoding said mannanase.


SUMMARY OF THE INVENTION

It is an object of the present invention to prepare a single-component mannanase.
Accordingly, the present invention relates to an enzyme exhibiting mannanase activity, which enzyme mannanase derived from Aspergillus aculeatus, CBS 101.43, or an analogue of said sequence, and/or being at least 80% homologous thereto.
In the present context, the term "derived from" is intended not only to indicate a mannanase produced by strain CBS 101.43, but also a mannanase encoded by a DNA sequence isolated from strain CBS 101.43 and produced in a host organism transformed with said DNA sequence.
The term "analogue" is intended to indicate a DNA sequence which hybridizes with the same oligonucleotide probe as the DNA sequence shown in SEQ ID No. 1 under certain specified conditions (such as presoaking in 5.times.SSC and prehybridizing for 1 h at .about.40.degree. C. in a solution of 5.times.SSC, 5.times.Denhardt's solution, 50 mM sodium phosphate, pH 6.8, and 50 .mu.g of denatured sonicated calf thymus DNA, followed by hybridization in the same solution supplemented with 50 .mu.Ci 32-P-dCTP labelled probe for 18 h at .about.40.degree. C. followed by washing three times in 2.times.SSC, 0.2% SDS at 40.degree. C. f

REFERENCES:
Christgau et al. (1994) Biochem. Mol. Biol. Int. 33(5): 917-925.
Murao et al. (1979) J. Ferment. Technol. 57(3): 151-156.
Harris, ELV (1989) In: Protein Purification Methods: A Practical Approach, Haris, ELV and S Angal, eds. IRL Press, Oxford.
Janson, J. (1984) Trends in Biotechnology 2(2): 31-38.
JP Abstract 63209586, Aug. 31, 1988, Derwent Database Week 8841.

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